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Conserved domains on  [gi|15599169|ref|NP_252663|]
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lost adherence sensor LadS [Pseudomonas aeruginosa PAO1]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 13737002)

hybrid sensor histidine kinase/response regulator with seven transmembrane region and extracellular sensor domain, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
403-784 9.73e-72

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 252.85  E-value: 9.73e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  403 RKLEAlnqelansNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQA 482
Cdd:PRK11107 285 RAQEA--------ARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  483 GKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVA-A 561
Cdd:PRK11107 357 GKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVElR 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  562 GRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGS--RFLL 639
Cdd:PRK11107 437 ALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGStfWFHL 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  640 RLQLTQPAQGLAPP-------------PRRAGGQAVRR------------------------------------------ 664
Cdd:PRK11107 517 PLDLNPNPIIDGLPtdclagkrllyvePNSAAAQATLDilsetplevtysptlsqlpeahydilllglpvtfrepltmlh 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 -----------------------------------------------------------------PEEC---TVLVVEDN 676
Cdd:PRK11107 597 erlakaksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptDESRlplTVMAVDDN 676
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  677 AIN-QLVtrGMLLK-LGYRVRTADNGSEALElLARERP-DGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTAHSHS 753
Cdd:PRK11107 677 PANlKLI--GALLEeQVEHVVLCDSGHQAVE-QAKQRPfDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMA 753
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15599169  754 GDRERCLAAGMSDYMAKPVKFEELQTLLHDW 784
Cdd:PRK11107 754 GERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
182-386 1.07e-61

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


:

Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 206.36  E-value: 1.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   182 RIYVLGIIYGVLLVMLIYNLFIFLSVRDTSYLYYILYIASFGLYQVSVNGAGIEYFWPDSPWWANAATP--FLIGSAALF 259
Cdd:pfam07695   1 ENLLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLylSLLLLLPFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   260 GCQFARSFLHTRDHSVWVDRGLLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIA 339
Cdd:pfam07695  81 ALLFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKGYKPARYFLLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15599169   340 WTAFLLGGIVNTLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADR 386
Cdd:pfam07695 161 WLLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALADR 207
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
34-166 4.85e-42

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 429601  Cd Length: 127  Bit Score: 149.41  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169    34 IDVFEDVRGSADINDITSRaiDSSFRRHDKDVLNAGYSRSVFWLRLDLDYrpvASSDPRTWLLELAYPPLDKLDLYLPDG 113
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSA--DGRFRPPEKGVPNFGYSSSAYWLRFTLEN---PTDAPKDWLLELAYPLLDEIDLYLPDG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15599169   114 QGGYRlAQRTGDTLPFASRPIRQNNYLFELGLEPNKPQRVYLRLESQGSIQAP 166
Cdd:pfam07696  76 GGGYR-EQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVTLYLRVKSSGSLLLP 127
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
403-784 9.73e-72

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 252.85  E-value: 9.73e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  403 RKLEAlnqelansNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQA 482
Cdd:PRK11107 285 RAQEA--------ARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  483 GKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVA-A 561
Cdd:PRK11107 357 GKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVElR 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  562 GRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGS--RFLL 639
Cdd:PRK11107 437 ALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGStfWFHL 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  640 RLQLTQPAQGLAPP-------------PRRAGGQAVRR------------------------------------------ 664
Cdd:PRK11107 517 PLDLNPNPIIDGLPtdclagkrllyvePNSAAAQATLDilsetplevtysptlsqlpeahydilllglpvtfrepltmlh 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 -----------------------------------------------------------------PEEC---TVLVVEDN 676
Cdd:PRK11107 597 erlakaksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptDESRlplTVMAVDDN 676
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  677 AIN-QLVtrGMLLK-LGYRVRTADNGSEALElLARERP-DGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTAHSHS 753
Cdd:PRK11107 677 PANlKLI--GALLEeQVEHVVLCDSGHQAVE-QAKQRPfDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMA 753
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15599169  754 GDRERCLAAGMSDYMAKPVKFEELQTLLHDW 784
Cdd:PRK11107 754 GERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
404-646 5.77e-64

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 214.00  E-value: 5.77e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 404 KLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQ--TVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQ 481
Cdd:COG2205   1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLdeEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 482 AGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAA 561
Cdd:COG2205  81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGG-TITISA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 562 GRTHDGValRVEVIDTGIGFDMAAGSDLYQRFVQADSslTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:COG2205 159 RREGDGV--RISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234

                ....*
gi 15599169 642 QLTQP 646
Cdd:COG2205 235 PLAES 239
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
182-386 1.07e-61

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 206.36  E-value: 1.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   182 RIYVLGIIYGVLLVMLIYNLFIFLSVRDTSYLYYILYIASFGLYQVSVNGAGIEYFWPDSPWWANAATP--FLIGSAALF 259
Cdd:pfam07695   1 ENLLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLylSLLLLLPFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   260 GCQFARSFLHTRDHSVWVDRGLLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIA 339
Cdd:pfam07695  81 ALLFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKGYKPARYFLLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15599169   340 WTAFLLGGIVNTLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADR 386
Cdd:pfam07695 161 WLLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALADR 207
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
670-781 3.50e-49

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 168.80  E-value: 3.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALP-GCAELPVLALT 748
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEgGGRRTPIIALT 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
34-166 4.85e-42

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 149.41  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169    34 IDVFEDVRGSADINDITSRaiDSSFRRHDKDVLNAGYSRSVFWLRLDLDYrpvASSDPRTWLLELAYPPLDKLDLYLPDG 113
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSA--DGRFRPPEKGVPNFGYSSSAYWLRFTLEN---PTDAPKDWLLELAYPLLDEIDLYLPDG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15599169   114 QGGYRlAQRTGDTLPFASRPIRQNNYLFELGLEPNKPQRVYLRLESQGSIQAP 166
Cdd:pfam07696  76 GGGYR-EQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVTLYLRVKSSGSLLLP 127
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
421-637 1.52e-30

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 123.09  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   421 EFLATVTHELRTPMSGVIGSLELMQTVPMDV--ELAEYQRTAAGSARDMMRMVNDILALIELQAGKLYPRREPFSLRGLF 498
Cdd:TIGR02966 116 DFVANVSHELRTPLTVLRGYLETLADGPDEDpeEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   499 DSLRAQYAPRVEEKGLRFALQLDDSLPdtLEGDAGKLAQALGYLVDNAIKFT-ARGSVTLRvaAGRTHDGValRVEVIDT 577
Cdd:TIGR02966 196 DHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVR--WRRDGGGA--EFSVTDT 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   578 GIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRF 637
Cdd:TIGR02966 270 GIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
670-781 1.61e-30

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 115.71  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 15599169   750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
530-644 1.33e-29

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.13  E-value: 1.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169    530 GDAGKLAQALGYLVDNAIKFT-ARGSVTLRVaagrTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSlTRGYGGLG 608
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 15599169    609 IGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLT 644
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
402-641 3.15e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 100.67  E-value: 3.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  402 SRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQ--TVPMDVE-LAEYQRtaagSARDMMRMVNDILALI 478
Cdd:NF012163 223 AQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQdgIRKFTPEsLDSLQA----EVGTLTKLVDDLHDLS 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  479 ELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLpdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLR 558
Cdd:NF012163 299 MSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG-SLH 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  559 VAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFL 638
Cdd:NF012163 376 ISASQRPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                 ...
gi 15599169  639 LRL 641
Cdd:NF012163 454 VTL 456
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
383-665 1.26e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 96.25  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  383 LADRINAMkeerARILQESSRKLEALNqelansnRLKDEFLATVTHELRTPMSgvigslelmqTVPMDVELAEYQR---- 458
Cdd:NF040691 246 LARSFNQM----ADSLQRQIRQLEELS-------RLQQRFVSDVSHELRTPLT----------TIRMAADVIHDSRddfd 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  459 -TAAGSARDMM-------RMVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSlPDTLEG 530
Cdd:NF040691 305 pATARSAELLHteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEV 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  531 DAGKLAQALGYLVDNAIKFTARGSVTLRVAAgrthDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIG 610
Cdd:NF040691 384 DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQ----DDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLG 459
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15599169  611 LALCRKLVELLGGELTHESRPGQGSRFLLRLqltqpaqglappPRRAGGQAVRRP 665
Cdd:NF040691 460 LAIALEDARLHGGWLEAWGRPGQGSQFRLTL------------PRVAGDRLTTSP 502
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
424-641 1.32e-07

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 54.23  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  424 ATVTHELRTPMSGVIGSLE------------LMQTVPMDVE----LAEYQRTaagsardmmrmvndiLALIELQAGKLyp 487
Cdd:NF012226 143 AAIAHELRTPITILQGRLQgildgvfepdpaLFKSLLNQVEglshLVEDLRT---------------LSLVENQQLRL-- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  488 RREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDslpDTLEGDAGKLAQALGYLVDNAIKFTARGsvTLRVAAGRTHDG 567
Cdd:NF012226 206 NYESVDLKDSIEKVLKMFEDRLEQAQLTIVLNLTA---TPVFCDRRRIEQVLIALIDNAIRYANAG--KLKISSSVIQDD 280
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599169  568 VALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHeSRPGQGSRFLLRL 641
Cdd:NF012226 281 WILQIE--DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIKL 351
Trep_Strep TIGR02185
putative ECF transporter S component, Trep_Strep family; This family consists of strongly ...
281-381 4.03e-03

putative ECF transporter S component, Trep_Strep family; This family consists of strongly hydrophobic proteins about 190 amino acids in length with a strongly basic motif near the C-terminus. If is found in rather few species, but in paralogous families of 12 members in the oral pathogenic spirochaete Treponema denticola and 2 in Streptococcus pneumoniae R6. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 274019  Cd Length: 189  Bit Score: 39.19  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   281 LLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIfaAGILAWLRGMRVARYfiiaWTAFLLGGIvntLMVLGYLPN 360
Cdd:TIGR02185   8 FIGLLTAIYFAIQFIVGMLTMTTGFFAHLFSPGITAFL--VGIIFFLMVAKVPKR----GVIFIFGIL---LGLLFFLMG 78
                          90       100
                  ....*....|....*....|..
gi 15599169   361 MFLTM-YASQIGSALEVGLLSL 381
Cdd:TIGR02185  79 MYWPMiISSIIGGLLADIIAST 100
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
403-784 9.73e-72

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 252.85  E-value: 9.73e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  403 RKLEAlnqelansNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQA 482
Cdd:PRK11107 285 RAQEA--------ARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  483 GKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVA-A 561
Cdd:PRK11107 357 GKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVElR 436
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  562 GRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGS--RFLL 639
Cdd:PRK11107 437 ALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGStfWFHL 516
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  640 RLQLTQPAQGLAPP-------------PRRAGGQAVRR------------------------------------------ 664
Cdd:PRK11107 517 PLDLNPNPIIDGLPtdclagkrllyvePNSAAAQATLDilsetplevtysptlsqlpeahydilllglpvtfrepltmlh 596
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 -----------------------------------------------------------------PEEC---TVLVVEDN 676
Cdd:PRK11107 597 erlakaksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptDESRlplTVMAVDDN 676
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  677 AIN-QLVtrGMLLK-LGYRVRTADNGSEALElLARERP-DGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTAHSHS 753
Cdd:PRK11107 677 PANlKLI--GALLEeQVEHVVLCDSGHQAVE-QAKQRPfDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAHAMA 753
                        490       500       510
                 ....*....|....*....|....*....|.
gi 15599169  754 GDRERCLAAGMSDYMAKPVKFEELQTLLHDW 784
Cdd:PRK11107 754 GERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
404-646 5.77e-64

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 214.00  E-value: 5.77e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 404 KLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQ--TVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQ 481
Cdd:COG2205   1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLdeEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 482 AGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAA 561
Cdd:COG2205  81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGG-TITISA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 562 GRTHDGValRVEVIDTGIGFDMAAGSDLYQRFVQADSslTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:COG2205 159 RREGDGV--RISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234

                ....*
gi 15599169 642 QLTQP 646
Cdd:COG2205 235 PLAES 239
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
310-641 4.19e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 214.77  E-value: 4.19e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 310 LALAFTGLIFAAGILAWLRGMRVARYFIIAWTAFLLGGIVNTLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADRINA 389
Cdd:COG0642   1 LLLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 390 MKEERARILQESSRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPmDVELAEYQRTAAGSARDMMR 469
Cdd:COG0642  81 LLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL-DEEQREYLETILRSADRLLR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 470 MVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKF 549
Cdd:COG0642 160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKY 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 550 TARGS-VTLRVaagrTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSltRGYGGLGIGLALCRKLVELLGGELTHE 628
Cdd:COG0642 239 TPEGGtVTVSV----RREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVE 312
                       330
                ....*....|...
gi 15599169 629 SRPGQGSRFLLRL 641
Cdd:COG0642 313 SEPGKGTTFTVTL 325
7TMR-DISM_7TM pfam07695
7TM diverse intracellular signalling; This entry represents the transmembrane region of the ...
182-386 1.07e-61

7TM diverse intracellular signalling; This entry represents the transmembrane region of the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules).


Pssm-ID: 429600 [Multi-domain]  Cd Length: 207  Bit Score: 206.36  E-value: 1.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   182 RIYVLGIIYGVLLVMLIYNLFIFLSVRDTSYLYYILYIASFGLYQVSVNGAGIEYFWPDSPWWANAATP--FLIGSAALF 259
Cdd:pfam07695   1 ENLLLGLFYGILLALALYNLFLFFSLRDRSYLYYVLYLLSFLLYQLSLNGLGFQYLWPNAPPWLNNKLLylSLLLLLPFF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   260 GCQFARSFLHTRDHSVWVDRGLLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIA 339
Cdd:pfam07695  81 ALLFARSFLELKKYLPRLLRLLLGLALLLALLLLLLPLFPYTLSLPLAQLLALLFILFLLLLGIIAWRKGYKPARYFLLA 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 15599169   340 WTAFLLGGIVNTLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADR 386
Cdd:pfam07695 161 WLLLLIGALIDILSLLGLLPSNFFTNYLLQIGSALEVLLLSLALADR 207
PRK15347 PRK15347
two component system sensor kinase;
400-777 2.49e-60

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 220.28  E-value: 2.49e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  400 ESSRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIE 479
Cdd:PRK15347 379 ERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSR 458
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  480 LQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRV 559
Cdd:PRK15347 459 IESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRV 538
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  560 AagRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLtrgyGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLL 639
Cdd:PRK15347 539 K--RHEQQLCFTVE--DTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSL 610
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  640 RLQLTQPAQ---------------------GLAPPP--------------------RRAGGQAVRRPEECT--------- 669
Cdd:PRK15347 611 VLPLNEYAPpeplkgelsaplalhrqlsawGITCQPghqnpalldpelaylpgrlyDLLQQIIQGAPNEPVinlplqpwq 690
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 --VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGC--AELPVL 745
Cdd:PRK15347 691 lqILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNldPDCMIV 770
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15599169  746 ALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK15347 771 ALTANAAPEEIHRCKKAGMNHYLTKPVTLAQL 802
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
281-641 4.44e-59

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 205.94  E-value: 4.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 281 LLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIAWTAFLLGGIVNTLMVLGYLPN 360
Cdd:COG5002  23 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 361 MFLTMYASQIGSALEVGLLSLALADRINAMKEERARILQESSRKLEALNQ----ELANSNRLKDEFLATVTHELRTPMSG 436
Cdd:COG5002 103 ILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVErditELERLEQMRREFVANVSHELRTPLTS 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 437 VIGSLELMQT--VPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGL 514
Cdd:COG5002 183 IRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGI 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 515 RFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGValRVEVIDTGIGFDMAAGSDLYQRFV 594
Cdd:COG5002 263 ELELDLPEDPL-LVLGDPDRLEQVLTNLLDNAIKYTPEGG-TITVSLREEDDQV--RISVRDTGIGIPEEDLPRIFERFY 338
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15599169 595 QADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:COG5002 339 RVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
412-783 1.56e-55

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 204.79  E-value: 1.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  412 LANSNRLKDEFLATVTHELRTPMSGVIG-SLELMQTvPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAGKLYPRRE 490
Cdd:PRK11091 276 LEKASRDKTTFISTISHELRTPLNGIVGlSRILLDT-ELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQ 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  491 PFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVAAgrtHDGVAL 570
Cdd:PRK11091 355 PIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRY---EEGDML 431
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  571 RVEVIDTGIG---------FDMaagsdLYQrfVQaDSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:PRK11091 432 TFEVEDSGIGipedeldkiFAM-----YYQ--VK-DSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTI 503
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  642 QLTQPAQGLAPPPRRAGGQAVRrpeeCTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQM 721
Cdd:PRK11091 504 HAPAVAEEVEDAFDEDDMPLPA----LNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQL 579
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599169  722 PVMDGFATCRAIRALPGCAELPVL-ALTAHSHSgDRERCLAAGMSDYMAKPVKFEELQTLLHD 783
Cdd:PRK11091 580 PDMTGLDIARELRERYPREDLPPLvALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKK 641
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
401-781 2.37e-53

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 199.81  E-value: 2.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  401 SSR-KLEALNQELAN----SNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDIL 475
Cdd:PRK10841 424 SARvKMEESLQEMAQaaeqASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDIL 503
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  476 AL--IELQAGKLYPRrePFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARG 553
Cdd:PRK10841 504 DFskIESEQLKIEPR--EFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTG 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  554 SVTLRVaaGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQ 633
Cdd:PRK10841 582 CIVLHV--RVDGDYLSFRVR--DTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGM 657
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  634 GSRFLLRLQLTQpAQGLAPPP--------------------------RRAGGQAVRRPEECT------------------ 669
Cdd:PRK10841 658 GSQFTIRIPLYG-AQYPQKKGveglqgkrcwlavrnasleqfletllQRSGIQVQRYEGQEPtpedvlitddpvqkkwqg 736
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 -------------------------------------------------------------------VLVVEDNAINQLV 682
Cdd:PRK10841 737 ravitfcrrhigipleiapgewvhstatphelpallariyrielesddsanalpstdkavsdnddmmILVVDDHPINRRL 816
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  683 TRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpGCAeLPVLALTAHSHSGDRERCLAA 762
Cdd:PRK10841 817 LADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL-GLT-LPVIGVTANALAEEKQRCLEA 894
                        490
                 ....*....|....*....
gi 15599169  763 GMSDYMAKPVKFEELQTLL 781
Cdd:PRK10841 895 GMDSCLSKPVTLDVLKQTL 913
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
387-785 1.23e-52

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 197.44  E-value: 1.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  387 INAMKEERARILQESSRKLEAL-------NQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRT 459
Cdd:PRK11466 405 LNRHREQLAAQVKARTAELQELviehrqaRAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRA 484
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  460 AAGSARDMMRMVNDIL--ALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQ 537
Cdd:PRK11466 485 ITDSGESLLTILNDILdySAIEAGGKNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQ 564
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  538 ALGYLVDNAIKFTARGSVTLRVAAgrthDGVALRVEVIDTGIGFDMAAGSDLYQRFVQadssLTRGYGGLGIGLALCRKL 617
Cdd:PRK11466 565 VITNLLSNALRFTDEGSIVLRSRT----DGEQWLVEVEDSGCGIDPAKLAEIFQPFVQ----VSGKRGGTGLGLTISSRL 636
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  618 VELLGGELTHESRPGQGSRFLLRLQLTQPaqglAPPPRRAGGQAVRRpEECTVLVVEDNAINQLVTRGMLLKLGYRVRTA 697
Cdd:PRK11466 637 AQAMGGELSATSTPEVGSCFCLRLPLRVA----TAPVPKTVNQAVRL-DGLRLLLIEDNPLTQRITAEMLNTSGAQVVAV 711
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  698 DNGSEALELLARERP-DGVLLDCQMPVMDGFATCRAI-RALPgcaELPVLALTAH---SHSGDRERCLAAGMsdyMAKPV 772
Cdd:PRK11466 712 GNAAQALETLQNSEPfAAALVDFDLPDYDGITLARQLaQQYP---SLVLIGFSAHvidETLRQRTSSLFRGI---IPKPV 785
                        410
                 ....*....|...
gi 15599169  773 KFEELQTLLHDWL 785
Cdd:PRK11466 786 PREVLGQLLAHYL 798
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
670-781 3.50e-49

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 168.80  E-value: 3.50e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALP-GCAELPVLALT 748
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEgGGRRTPIIALT 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:cd17546  81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
535-643 2.38e-48

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 166.13  E-value: 2.38e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARGSVTLRVAA-GRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLAL 613
Cdd:cd16922   1 LRQILLNLLGNAIKFTEEGEVTLRVSLeEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 614 CRKLVELLGGELTHESRPGQGSRFLLRLQL 643
Cdd:cd16922  81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
669-785 5.15e-46

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 160.40  E-value: 5.15e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:COG0784   7 RILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALT 86
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWL 785
Cdd:COG0784  87 AYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
7TMR-DISMED2 pfam07696
7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular ...
34-166 4.85e-42

7TMR-DISM extracellular 2; This entry represents one of two distinct types of extracellular domain found in the 7TM-DISM (7TM Receptors with Diverse Intracellular Signalling Modules) bacterial transmembrane proteins. It is possible that this domain adopts a jelly roll fold and acts as a receptor for carbohydrates and their derivatives. It can also recognize Ca(II) (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 429601  Cd Length: 127  Bit Score: 149.41  E-value: 4.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169    34 IDVFEDVRGSADINDITSRaiDSSFRRHDKDVLNAGYSRSVFWLRLDLDYrpvASSDPRTWLLELAYPPLDKLDLYLPDG 113
Cdd:pfam07696   1 VEYLEDPTGSLTIEDVLSA--DGRFRPPEKGVPNFGYSSSAYWLRFTLEN---PTDAPKDWLLELAYPLLDEIDLYLPDG 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15599169   114 QGGYRlAQRTGDTLPFASRPIRQNNYLFELGLEPNKPQRVYLRLESQGSIQAP 166
Cdd:pfam07696  76 GGGYR-EQRLGDRLPFSQRPVAHRNFVFPLPLPPGETVTLYLRVKSSGSLLLP 127
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
405-781 1.20e-41

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 164.91  E-value: 1.20e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   405 LEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVEL-AEYQRTAAGSARDMMRMVNDILALIELQAG 483
Cdd:PRK09959  698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATGQSLLGLIGEILDVDKIESG 777
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   484 KLYPRREPFSLRGLFDSLRAQYAPRVEEKGLrfALQLDDSLPD--TLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVAA 561
Cdd:PRK09959  778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSI--ALSCSSTFPDhyLVKIDPQAFKQVLSNLLSNALKFTTEGAVKITTSL 855
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   562 GRTHDGVA-LRVEVIDTGIGFDMAAGSDLYQRFVQadSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLR 640
Cdd:PRK09959  856 GHIDDNHAvIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTIT 933
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   641 LQLtQPAQGLAPPPRRAGgQAVRRPEECTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQ 720
Cdd:PRK09959  934 IPV-EISQQVATVEAKAE-QPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVN 1011
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599169   721 MPVMDGFATCRAIRALPgcAELPVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:PRK09959 1012 MPNMDGFELTRKLREQN--SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL 1070
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
150-641 2.83e-41

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 158.41  E-value: 2.83e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 150 PQRVYLRLESQGSIQAPLTLWSPKAYLEEQPERIYVLGIIYGVLLVMLIYNLFIFLSVRDTSYLYYILYIASFGLYQVSV 229
Cdd:COG4251  13 LLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 230 NGAGIEYFWPDSPWWANAATPFLIGSAALFGCQFARSFLHTRDHSVWVDRGLLALMAVGALVMLMALTMSYAVALRLATY 309
Cdd:COG4251  93 LLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 310 LALAFTGLIFAAGILAWLRGMRVARYFIIAWTAFLLGGIVNTLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADRINA 389
Cdd:COG4251 173 AALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVL 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 390 MKEERARILQESSRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVP---MDVELAEYQRTAAGSARD 466
Cdd:COG4251 253 ELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYgdkLDEEGREYLERIRDAAER 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 467 MMRMVNDILALieLQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALqldDSLPdTLEGDAGKLAQALGYLVDNA 546
Cdd:COG4251 333 MQALIDDLLAY--SRVGRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEV---GPLP-TVRGDPTLLRQVFQNLISNA 406
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 547 IKFTARGSV-TLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSltRGYGGLGIGLALCRKLVELLGGEL 625
Cdd:COG4251 407 IKYSRPGEPpRIEIGAEREGGEWVFSVR--DNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRI 482
                       490
                ....*....|....*.
gi 15599169 626 THESRPGQGSRFLLRL 641
Cdd:COG4251 483 WVESEPGEGATFYFTL 498
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
669-781 5.59e-41

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 148.13  E-value: 5.59e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:COG3706   3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLT 82
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:COG3706  83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
663-785 1.06e-36

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 137.60  E-value: 1.06e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 663 RRPEECTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAEL 742
Cdd:COG3437   2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDI 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599169 743 PVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWL 785
Cdd:COG3437  82 PVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
669-777 7.03e-35

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 131.62  E-value: 7.03e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:COG0745   3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIMLT 80
                        90       100
                ....*....|....*....|....*....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:COG0745  81 ARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
669-778 7.66e-34

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 125.35  E-value: 7.66e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:cd17548   1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17548  81 AYAMKGDREKILEAGCDGYISKPIDTREFL 110
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
670-781 1.28e-31

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 119.10  E-value: 1.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:cd17580  81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
669-772 1.39e-30

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 115.67  E-value: 1.39e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMIT 80
                        90       100
                ....*....|....*....|....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPV 772
Cdd:cd17538  81 ALDDREDRIRGLEAGADDFLSKPI 104
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
421-637 1.52e-30

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 123.09  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   421 EFLATVTHELRTPMSGVIGSLELMQTVPMDV--ELAEYQRTAAGSARDMMRMVNDILALIELQAGKLYPRREPFSLRGLF 498
Cdd:TIGR02966 116 DFVANVSHELRTPLTVLRGYLETLADGPDEDpeEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   499 DSLRAQYAPRVEEKGLRFALQLDDSLPdtLEGDAGKLAQALGYLVDNAIKFT-ARGSVTLRvaAGRTHDGValRVEVIDT 577
Cdd:TIGR02966 196 DHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTITVR--WRRDGGGA--EFSVTDT 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   578 GIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRF 637
Cdd:TIGR02966 270 GIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
670-781 1.61e-30

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 115.71  E-value: 1.61e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTA 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 15599169   750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:pfam00072  79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
670-772 1.11e-29

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 113.37  E-value: 1.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                        90       100
                ....*....|....*....|...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPV 772
Cdd:cd19920  81 LTDTEDKVKGFELGAVDYITKPF 103
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
530-644 1.33e-29

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.13  E-value: 1.33e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169    530 GDAGKLAQALGYLVDNAIKFT-ARGSVTLRVaagrTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSlTRGYGGLG 608
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTL----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGTG 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 15599169    609 IGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLT 644
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
410-648 3.15e-29

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 121.22  E-value: 3.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 410 QELANSNRLKD--EFLATVTHELRTPMSGVIGSLELMQ------TVPMDVELAEYQRTAAGSARDMMRMVNDILALielq 481
Cdd:COG5000 190 TELLRAERLAAwgELARRIAHEIKNPLTPIQLSAERLRrkladkLEEDREDLERALDTIIRQVDRLKRIVDEFLDF---- 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 482 AGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAA 561
Cdd:COG5000 266 ARLPEPQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIEEGG-EIEVST 343
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 562 GRTHDGValRVEVIDTGIGFDMAAGSDLYQRFVQadsslTRGyGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:COG5000 344 RREDGRV--RIEVSDNGPGIPEEVLERIFEPFFT-----TKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415

                ....*..
gi 15599169 642 QLTQPAQ 648
Cdd:COG5000 416 PLAEEAE 422
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
671-771 4.57e-29

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 111.17  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 671 LVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTAH 750
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELP--PDIPVIVLTAK 78
                        90       100
                ....*....|....*....|.
gi 15599169 751 SHSGDRERCLAAGMSDYMAKP 771
Cdd:cd00156  79 ADEEDAVRALELGADDYLVKP 99
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
281-641 1.10e-28

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 118.36  E-value: 1.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 281 LLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIAWTAFLLGGIVNTLMVLGYLPN 360
Cdd:COG4191   3 RLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 361 MFLTMYASQIGSALEVGLLSLALADRINAMkEERARILQESSRKLEALNQELANSNRLKD--EFLATVTHELRTPMSGVI 438
Cdd:COG4191  83 GLLLLLLLEALLLLLLAALDAEENAELEEL-ERDITELERAEEELRELQEQLVQSEKLAAlgELAAGIAHEINNPLAAIL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 439 GSLELM----QTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAgklyPRREPFSLRGLFDSLRAQYAPRVEEKGL 514
Cdd:COG4191 162 GNAELLrrrlEDEPDPEELREALERILEGAERAAEIVRSLRAFSRRDE----EEREPVDLNELIDEALELLRPRLKARGI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 515 RFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIK-FTARGSVTLRVAAGRTHDGValRVEVIDTGIGFDMAAGSDLYQRF 593
Cdd:COG4191 238 EVELDLPPDLP-PVLGDPGQLEQVLLNLLINAIDaMEEGEGGRITISTRREGDYV--VISVRDNGPGIPPEVLERIFEPF 314
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15599169 594 VqadssLTRGYG-GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:COG4191 315 F-----TTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
370-643 1.15e-27

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 117.25  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  370 IGSALEVGLL-------SLA-LADRINAMKE-ERARILQESSRKLEALNQELAnSNRLKDE-------FLATVTHELRTP 433
Cdd:PRK11100 192 LGIALLIGAGvvwwlnrSIRrLTRYADAVTEgKPVPLPKLGSSELRELAQALE-SMRVKLEgkayveqYVQTLTHELKSP 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  434 MSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKG 513
Cdd:PRK11100 271 LAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKG 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  514 LRFALQLDDSlpdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRF 593
Cdd:PRK11100 351 ITLRLRPDDA---RVLGDPFLLRQALGNLLDNAIDFSPEGG-TITLSAEVDGEQVALSVE--DQGPGIPDYALPRIFERF 424
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599169  594 VqadsSLTRGYGGL---GIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQL 643
Cdd:PRK11100 425 Y----SLPRPANGRkstGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
669-779 2.56e-27

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 107.14  E-value: 2.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGY-RVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLAL 747
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMI 81
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKPVKFEELQT 779
Cdd:cd17551  82 TADTDREVRLRALEAGATDFLTKPFDPVELLA 113
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
530-645 1.75e-26

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 104.37  E-value: 1.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   530 GDAGKLAQALGYLVDNAIKFTAR-GSVTLRVaagrtHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSsltRGYGGLG 608
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKaGEITVTL-----SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTG 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15599169   609 IGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLTQ 645
Cdd:pfam02518  73 LGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
669-785 3.85e-26

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 111.98  E-value: 3.85e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:COG2204   4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALD--PDLPVILLT 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWL 785
Cdd:COG2204  82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
671-771 6.72e-26

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 102.10  E-value: 6.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 671 LVVEDNA-INQLVTRgMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:cd17574   1 LVVEDDEeIAELLSD-YLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKG--SDIPIIMLTA 77
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17574  78 KDEEEDKVLGLELGADDYITKP 99
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
351-641 2.16e-24

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 107.09  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   351 TLMVLGYLPNMFLTMYASQIGSALEVGLLSLALADRINAMKEERARILQES-SRKLEALN-----QELANS-----NRLK 419
Cdd:TIGR01386 156 THLLDALRKWLILIAVLLVLLTALLGWWITRLGLEPLRRLSAVAARISPESlDQRLDPSRapaelRELAQSfnamlGRLE 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   420 D------EFLATVTHELRTPMSGVIGSLELMQTVPMDVElaEYQRTAAGSARD---MMRMVNDILALIELQAGKLYPRRE 490
Cdd:TIGR01386 236 DafqrlsQFSADLAHELRTPLTNLLGQTQVALSQPRTGE--EYREVLESNLEElerLSRMVSDMLFLARADNGQLALERV 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   491 PFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdtleGDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVAL 570
Cdd:TIGR01386 314 RLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGG-TITVRIERRSDEVRV 388
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599169   571 RVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESrPGQGSRFLLRL 641
Cdd:TIGR01386 389 SVS--NPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRF 456
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
669-785 3.35e-24

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 98.89  E-value: 3.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKL-GYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLA 746
Cdd:COG4565   5 RVLIVEDDPMVAELLRRYLERLpGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARG--PDVDVIV 82
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWL 785
Cdd:COG4565  83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
403-648 2.26e-23

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 102.62  E-value: 2.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 403 RKLEalnQELANSNRLKD--EFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIEL 480
Cdd:COG3852 120 KRLE---RELRRAEKLAAvgELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRP 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 481 QAgklyPRREPFSLRGLFDSLRAQYAPRVEeKGLRFALQLDDSLPDtLEGDAGKLAQALGYLVDNAIK-FTARGSVTLR- 558
Cdd:COG3852 197 RP----PEREPVNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRt 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 559 -----VAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVqadsSlTRGyGGLGIGLALCRKLVELLGGELTHESRPGQ 633
Cdd:COG3852 271 rverqVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF----T-TKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGK 344
                       250
                ....*....|....*
gi 15599169 634 GSRFLLRLQLTQPAQ 648
Cdd:COG3852 345 GTTFRIYLPLEQAEE 359
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
670-777 1.37e-22

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 93.60  E-value: 1.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDN-AINQLVTRGMLLKlGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALT 748
Cdd:cd17627   1 ILVVDDDrAVRESLRRSLRFE-GYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRA--AGNDLPILVLT 77
                        90       100
                ....*....|....*....|....*....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17627  78 ARDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
670-778 2.14e-22

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 93.00  E-value: 2.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKL-GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:cd17552   4 ILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLT 83
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPvkFEELQ 778
Cdd:cd17552  84 AKAQPSDRQRFASLGVAGVIAKP--FDPLT 111
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
669-784 2.37e-22

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 93.25  E-value: 2.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGML--LKLGYRVRTADNGSEALELLARE-------RPDGVLLDCQMPVMDGFATCRAIRALPGC 739
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFkeAGVPNELHVVRDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15599169 740 AELPVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL----QTLLHDW 784
Cdd:cd17557  81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFveaiRSLGEYW 129
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
402-641 3.15e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 100.67  E-value: 3.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  402 SRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQ--TVPMDVE-LAEYQRtaagSARDMMRMVNDILALI 478
Cdd:NF012163 223 AQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIQdgIRKFTPEsLDSLQA----EVGTLTKLVDDLHDLS 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  479 ELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLpdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLR 558
Cdd:NF012163 299 MSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG-SLH 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  559 VAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFL 638
Cdd:NF012163 376 ISASQRPKEVTLTVA--DSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIV 453

                 ...
gi 15599169  639 LRL 641
Cdd:NF012163 454 VTL 456
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
671-777 1.16e-21

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 90.80  E-value: 1.16e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 671 LVVEDNA-INQLVTRGmLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd19937   1 LVVDDEEdIVELLKYN-LEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTA 79
                        90       100
                ....*....|....*....|....*...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd19937  80 KGEEFDKVLGLELGADDYITKPFSPREL 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
670-786 1.83e-21

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 90.46  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWLL 786
Cdd:cd17598  81 LSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILV 117
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
669-771 8.67e-21

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 87.91  E-value: 8.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKL-GYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLA 746
Cdd:COG4753   1 KVLIVDDEPLIREGLKRILEWEaGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELD--PDTKIII 78
                        90       100
                ....*....|....*....|....*
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:COG4753  79 LSGYSDFEYAQEAIKLGADDYLLKP 103
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
383-665 1.26e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 96.25  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  383 LADRINAMkeerARILQESSRKLEALNqelansnRLKDEFLATVTHELRTPMSgvigslelmqTVPMDVELAEYQR---- 458
Cdd:NF040691 246 LARSFNQM----ADSLQRQIRQLEELS-------RLQQRFVSDVSHELRTPLT----------TIRMAADVIHDSRddfd 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  459 -TAAGSARDMM-------RMVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSlPDTLEG 530
Cdd:NF040691 305 pATARSAELLHteldrfeSLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEV 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  531 DAGKLAQALGYLVDNAIKFTARGSVTLRVAAgrthDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIG 610
Cdd:NF040691 384 DPRRVERVLRNLVVNAIEHGEGKPVVVTVAQ----DDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLG 459
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15599169  611 LALCRKLVELLGGELTHESRPGQGSRFLLRLqltqpaqglappPRRAGGQAVRRP 665
Cdd:NF040691 460 LAIALEDARLHGGWLEAWGRPGQGSQFRLTL------------PRVAGDRLTTSP 502
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
670-781 1.39e-20

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 87.84  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDG--VLLDCQMPVMDGFATCRAIRALPGCAELPVL-A 746
Cdd:cd19933   3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFqlVLLDLCMPEMDGFEVALRIRKLFGRRERPLIvA 82
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:cd19933  83 LTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
671-777 2.27e-19

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 84.19  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 671 LVVEDN-AINQLVTRgMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALTA 749
Cdd:cd17625   1 LVVEDEkDLSEAITK-HLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTA 77
                        90       100
                ....*....|....*....|....*...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17625  78 LDAVEDRVKGLDLGADDYLPKPFSLAEL 105
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
670-780 2.42e-19

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 84.22  E-value: 2.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLaRERPDG---VLLDCQMPVMDGFATCRAIRALPgcaELPVLA 746
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML-RENKDEfdlVITDVHMPDMDGFEFLELIRLEM---DLPVIM 76
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTL 780
Cdd:cd17584  77 MSADGSTSTVMKGLAHGACDYLLKPVSIEDLKNI 110
pleD PRK09581
response regulator PleD; Reviewed
669-773 2.54e-19

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 91.50  E-value: 2.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:PRK09581   4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVT 83
                         90       100
                 ....*....|....*....|....*
gi 15599169  749 AHSHSGDRERCLAAGMSDYMAKPVK 773
Cdd:PRK09581  84 ALDDPEDRVRGLEAGADDFLTKPIN 108
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
670-778 6.53e-19

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 82.92  E-value: 6.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNA-INQLVTRGmLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALT 748
Cdd:cd17624   1 ILLVEDDAlLGDGLKTG-LRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR--QGQSLPVLILT 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17624  78 ARDGVDDRVAGLDAGADDYLVKPFALEELL 107
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
403-648 7.92e-19

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 90.42  E-value: 7.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 403 RKLEalnQELANSNRLK--DEFLATVTHELRTPMSGVIGSLELMQTVPM-------DVELAEYQRtaagsardMMRMVND 473
Cdd:COG5809 255 KKLE---ELLRKSEKLSvvGELAAGIAHEIRNPLTSLKGFIQLLKDTIDeeqktylDIMLSELDR--------IESIISE 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 474 ILALIELQAGKLyprrEPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDtLEGDAGKLAQALGYLVDNAIKFTAR- 552
Cdd:COG5809 324 FLVLAKPQAIKY----EPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEg 398
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 553 GSVTLRVAAGRtHDGVALRveVIDTGIGFDMAAGSDLYQRFvqadssLTRGYGGLGIGLALCRKLVELLGGELTHESRPG 632
Cdd:COG5809 399 GNITIETKAED-DDKVVIS--VTDEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVG 469
                       250
                ....*....|....*.
gi 15599169 633 QGSRFLLRLQLTQPAQ 648
Cdd:COG5809 470 KGTTFSITLPIKLSEQ 485
PRK09303 PRK09303
histidine kinase;
408-637 2.03e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 88.08  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  408 LNQELAN-SNRL--KDEFLATVTHELRTPMSGV---IGSLELMQTVPMDVE----LAEYQRTAAGSARDMMRMVNDILal 477
Cdd:PRK09303 137 LRQENETlLEQLkfKDRVLAMLAHDLRTPLTAAslaLETLELGQIDEDTELkpalIEQLQDQARRQLEEIERLITDLL-- 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  478 ielQAGK-------LYPRRepFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFT 550
Cdd:PRK09303 215 ---EVGRtrwealrFNPQK--LDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKYT 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  551 -ARGSVTLrVAAGRTHDGValRVEVIDTGIGFDMAAGSDLYQ-RFVQADSSLTRGYGglgIGLALCRKLVELLGGELTHE 628
Cdd:PRK09303 289 pEGGTITL-SMLHRTTQKV--QVSICDTGPGIPEEEQERIFEdRVRLPRDEGTEGYG---IGLSVCRRIVRVHYGQIWVD 362

                 ....*....
gi 15599169  629 SRPGQGSRF 637
Cdd:PRK09303 363 SEPGQGSCF 371
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
422-649 2.23e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 88.92  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  422 FLATVTHELRTPMSGVIGSLELMQT---VPMDVELAEYQRTAAgsarDMMRMVNDILALIELQAGKLYPRREPFSLRGLF 498
Cdd:PRK10549 243 FMADISHELRTPLAVLRGELEAIQDgvrKFTPESVASLQAEVG----TLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLL 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  499 DSLRAQYAPRVEEKGLrfalQLDDSLPD--TLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviD 576
Cdd:PRK10549 319 EVAGGAFRERFASRGL----TLQLSLPDsaTVFGDPDRLMQLFNNLLENSLRYTDSGG-SLHISAEQRDKTLRLTFA--D 391
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599169  577 TGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLTQPAQG 649
Cdd:PRK10549 392 SAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQR 464
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
669-777 3.24e-18

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 81.14  E-value: 3.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDN-AINQLVtRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLAL 747
Cdd:cd17618   2 TILIVEDEpAIREMI-AFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17618  81 TARGEEEDKVRGLEAGADDYITKPFSPREL 110
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
669-781 6.64e-18

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 82.70  E-value: 6.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRV-RTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCaelPVLAL 747
Cdd:COG3707   5 RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA---PVILL 81
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:COG3707  82 TAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
402-717 8.75e-18

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 88.45  E-value: 8.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  402 SRKLEALNQELANSNRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQ 481
Cdd:PRK10618 433 NKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLE 512
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  482 AGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDTLEGDAGKLAQALGYLVDNAIKFTARGSVTLRVAA 561
Cdd:PRK10618 513 TQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQ 592
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  562 GRTHDGvALRVEVIDTGIGFDMAAGSDLYQRFVqADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:PRK10618 593 DESSPD-RLTIRILDTGAGVSIKELDNLHFPFL-NQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHL 670
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  642 QLTqpaqglaPPPRRAGGQAVRRPEECTVLV-VEDNAINQLVTRgMLLKLGYRVRTAD--NGSEALELLARERP-----D 713
Cdd:PRK10618 671 KML-------AADPEVEEEEEKLLDGVTVLLdITSEEVRKIVTR-QLENWGATCITPDerLISQEYDIFLTDNPsnltaS 742

                 ....
gi 15599169  714 GVLL 717
Cdd:PRK10618 743 TLLL 746
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
669-779 1.00e-17

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 79.37  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRV-RTADNGSEALELLARERPDGVLLDCQMP-VMDGFATCRAIRALPGcaeLPVLA 746
Cdd:cd17534   2 KILIVEDEAIIALDLKEILESLGYEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD---IPVIF 78
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQT 779
Cdd:cd17534  79 LTAYSDEETLERAKETNPYGYLVKPFNERELKA 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
669-777 2.41e-17

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 78.55  E-value: 2.41e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDN-AINQLVTrgMLLKL-GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGcaELPVLA 746
Cdd:cd17615   1 RVLVVDDEpNITELLS--MALRYeGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP--DVPVLF 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17615  77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
670-771 2.99e-17

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 78.59  E-value: 2.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYR--VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLAL 747
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTPVVMV 79
                        90       100
                ....*....|....*....|....*.
gi 15599169 748 TAHSHSGDRE--RCLAAGMSDYMAKP 771
Cdd:cd17541  80 SSLTEEGAEItlEALELGAVDFIAKP 105
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-641 3.24e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 77.89  E-value: 3.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIG 610
Cdd:cd16946   1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTPQEVRLDVE--DSAPGVSDDQLARLFERFYRVESSRNRASGGSGLG 77
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 611 LALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16946  78 LAICHNIALAHGGTISAEHSPLGGLRLVLTL 108
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-642 3.86e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 77.37  E-value: 3.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTaRGSVTLRVAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSltRGYGGLGIGLALC 614
Cdd:cd16921   1 LGQVLTNLLGNAIKFR-RPRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVGLAIV 77
                        90       100
                ....*....|....*....|....*...
gi 15599169 615 RKLVELLGGELTHESRPGQGSRFLLRLQ 642
Cdd:cd16921  78 RKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
375-777 4.11e-17

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 85.88  E-value: 4.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  375 EVGLLSLALADRINAMkeERARILQESsrklEALNQELANSNRLkdEFLAT----VTHELRTPMSGVIGSLELMQT-VPM 449
Cdd:PRK13837 410 ELQLLELALDCLAHAI--ERRRLETER----DALERRLEHARRL--EAVGTlasgIAHNFNNILGAILGYAEMALNkLAR 481
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  450 DVELAEYQRTAAGSARDMMRMVNDILALIELQAGklypRREPFSLRGLFD----SLRAQYAPRVEekglrFALQLDDSlP 525
Cdd:PRK13837 482 HSRAARYIDEIISAGARARLIIDQILAFGRKGER----NTKPFDLSELVTeiapLLRVSLPPGVE-----LDFDQDQE-P 551
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  526 DTLEGDAGKLAQALGYLVDNAIK-FTARGSVT--LRVAAGRTHDGVA-----------LRVEviDTGIGFDMAAGSDLYQ 591
Cdd:PRK13837 552 AVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDisLSRAKLRAPKVLShgvlppgryvlLRVS--DTGAGIDEAVLPHIFE 629
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  592 RFVQadsslTRGyGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLT-----QPAQGLAPP--PRRAGGqavrr 664
Cdd:PRK13837 630 PFFT-----TRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSskvpvAPQAFFGPGplPRGRGE----- 698
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 peecTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLAR--ERPDGVLLDCQMPVMDGFATcrAIRALpgcAEL 742
Cdd:PRK13837 699 ----TVLLVEPDDATLERYEEKLAALGYEPVGFSTLAAAIAWISKgpERFDLVLVDDRLLDEEQAAA--ALHAA---APT 769
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 15599169  743 PVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK13837 770 LPIILGGNSKTMALSPDLLASVAEILAKPISSRTL 804
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
670-777 4.72e-17

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 77.55  E-value: 4.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAinqLVTRGMLLKLGYR-----VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgCAELPV 744
Cdd:cd17535   1 VLIVDDHP---LVREGLRRLLESEpdievVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR--YPDLKV 75
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 745 LALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17535  76 IVLTAHDDPEYVLRALKAGAAGYLLKDSSPEEL 108
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
669-777 1.08e-16

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 76.49  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKK--PDLPVIICT 79
                        90       100
                ....*....|....*....|....*....
gi 15599169 749 AHSHSGDRERCLAAGmsDYMAKPVKFEEL 777
Cdd:cd17554  80 AYSEYKSDFSSWAAD--AYVVKSSDLTEL 106
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
668-778 1.23e-16

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 76.79  E-value: 1.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 668 CTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARErPDG--VLLDCQMPVMDGFATCRAIRALPGCAELPVL 745
Cdd:cd17544   1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIklVITDYNMPEMDGFELVREIRKKYSRDQLAII 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 746 ALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17544  80 GISASGDNALSARFIKAGANDFLTKPFLPEEFY 112
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
670-781 1.52e-16

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 76.22  E-value: 1.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNainQLVTRGMLL-----KLGYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAL-PGCael 742
Cdd:cd17536   1 VLIVDDE---PLIREGLKKlidweELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELyPDI--- 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599169 743 PVLALTAHShsgDRE---RCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:cd17536  75 KIIILSGYD---DFEyaqKAIRLGVVDYLLKPVDEEELEEAL 113
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
670-778 1.74e-16

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 75.92  E-value: 1.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVPIIMLTA 77
                        90       100
                ....*....|....*....|....*....
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17614  78 KDSEVDKVLGLELGADDYVTKPFSNRELL 106
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
670-777 3.29e-16

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 75.20  E-value: 3.29e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDN-AINQLVtrGMLLKL-GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGcaeLPVLAL 747
Cdd:cd17626   3 ILVVDDDaALAEMI--GIVLRGeGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG---VPIVML 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17626  78 TAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
669-777 1.58e-15

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 73.49  E-value: 1.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNA-INQLVtrGMLLK-LGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLA 746
Cdd:cd17562   2 KILAVDDSAsIRQMV--SFTLRgAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILM 79
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17562  80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
670-771 2.33e-15

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 72.20  E-value: 2.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRalpGCAELPVLALTA 749
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSA 77
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17620  78 RDEESDKIAALDAGADDYLTKP 99
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
670-780 5.27e-15

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 72.01  E-value: 5.27e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDG-----------VLLDCQMPVMDGFATCRAIRALPG 738
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDssnfnepkvnmIITDYCMPGMTGYDLLKKVKESSA 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599169 739 CAELPVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTL 780
Cdd:cd17581  81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKLADVKRL 122
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
670-771 9.15e-15

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 70.55  E-value: 9.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNA-INQLVTRGmLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:cd19935   1 ILVVEDEKkLAEYLKKG-LTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAG--KQTPVLMLT 77
                        90       100
                ....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19935  78 ARDSVEDRVKGLDLGADDYLVKP 100
PRK10490 PRK10490
sensor protein KdpD; Provisional
363-646 1.15e-14

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 78.15  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  363 LTMYASQIGSALEvgllSLALADRinamkEERARilqessrkLEALNQELANSnrlkdeFLATVTHELRTPMSGVIGSLE 442
Cdd:PRK10490 631 LETFTLLIANALE----RLTLTAS-----EEQAR--------LASEREQLRNA------LLAALSHDLRTPLTVLFGQAE 687
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  443 LMQtvpmdVELAEYQRTAAGSARDM-------MRMVNDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVeeKGLR 515
Cdd:PRK10490 688 ILT-----LDLASEGSPHARQASEIrqqvlntTRLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGL--SGHP 760
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  516 FALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTA-RGSVTLRVAAgrthDGVALRVEVIDTGIGFDMAAGSDLYQRFV 594
Cdd:PRK10490 761 INLSLPEPLT-LIHVDGPLFERVLINLLENAVKYAGaQAEIGIDAHV----EGERLQLDVWDNGPGIPPGQEQLIFDKFA 835
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599169  595 QAD--SSLTrgygGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLTQP 646
Cdd:PRK10490 836 RGNkeSAIP----GVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETP 885
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
422-641 1.16e-14

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 77.50  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  422 FLATVTHELRTPMSGVIGSLE--LMQT-VPMDVE------LAEYQRtaagsardMMRMVNDILALIELQAGKLYPRREPF 492
Cdd:PRK09835 265 FSADIAHEIRTPITNLITQTEiaLSQSrSQKELEdvlysnLEELTR--------MAKMVSDMLFLAQADNNQLIPEKKML 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  493 SLRG----LFDSLRAQyaprVEEKGLRfaLQLDDSlPDTLEGDAGKLAQALGYLVDNAIKFTARG-SVTLRVAagRTHDG 567
Cdd:PRK09835 337 DLADevgkVFDFFEAW----AEERGVE--LRFVGD-PCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQ--EVDHQ 407
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599169  568 VALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPgQGSRFLLRL 641
Cdd:PRK09835 408 VQLVVE--NPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISL 478
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
422-637 1.39e-14

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 76.59  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  422 FLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQ-RTAAGSARDMMRMVNDILALIELQAGKLYPRRE----PFSLRG 496
Cdd:PRK11006 207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKAlHTMREQTQRMEGLVKQLLTLSKIEAAPTIDLNEkvdvPMMLRV 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  497 LfdslrAQYAPRVEEKGLRFALQLDDSLpdTLEGDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviD 576
Cdd:PRK11006 287 L-----EREAQTLSQGKHTITFEVDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGT-HITVRWQRVPQGAEFSVE--D 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599169  577 TGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRF 637
Cdd:PRK11006 357 NGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRF 417
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
669-722 1.55e-14

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 68.36  E-value: 1.55e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15599169    669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMP 722
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
666-781 1.57e-14

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 76.61  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  666 EECTVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAL-PGcaeLPV 744
Cdd:PRK10365   4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALnPA---IPV 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15599169  745 LALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:PRK10365  81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATL 117
orf27 CHL00148
Ycf27; Reviewed
670-778 1.66e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.98  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:CHL00148   9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPIIMLTA 85
                         90       100
                 ....*....|....*....|....*....
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:CHL00148  86 LGDVSDRITGLELGADDYVVKPFSPKELE 114
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
669-782 1.69e-14

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 70.31  E-value: 1.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:cd17555   2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKES--PDTPVIVVS 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVkfEELQTLLH 782
Cdd:cd17555  80 GAGVMSDAVEALRLGAWDYLTKPI--EDLAVLEH 111
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
670-777 1.74e-14

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 70.41  E-value: 1.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNA-INQLVTRgMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcaELPVLALT 748
Cdd:cd17623   1 ILLIDDDReLTELLTE-YLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTS---QVPVLMLT 76
                        90       100
                ....*....|....*....|....*....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17623  77 ARGDDIDRILGLELGADDYLPKPFNPREL 105
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
405-641 2.36e-14

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 75.66  E-value: 2.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 405 LEALNQELANSNRLKDEfLATVTHELRTPMSgVIGSLelmqtvpmdVELAEYQrtaagsarDMMRMVNDILALIELQAGK 484
Cdd:COG3290 176 LERLEEELEGVKELAEA-LRAQRHDFRNHLH-TISGL---------LQLGEYD--------EALEYIDEISEELQELIDS 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 485 LYPRREPFSLRGLfdsLRAQYApRVEEKGLRFALQLDDSLPDtLEGDAGKLAQALGYLVDNAI-----KFTARGSVTLRV 559
Cdd:COG3290 237 LLSRIGNPVLAAL---LLGKAA-RARERGIDLTIDIDSDLPD-LPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSI 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 560 aagrTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVqadssLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLL 639
Cdd:COG3290 312 ----RDDGDELVIEVEDSGPGIPEELLEKIFERGF-----STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTV 382

                ..
gi 15599169 640 RL 641
Cdd:COG3290 383 RL 384
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
669-771 2.41e-14

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 73.07  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVEDN-AINQLVTRgMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLAL 747
Cdd:PRK11083   5 TILLVEDEqAIADTLVY-ALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFH--PALPVIFL 81
                         90       100
                 ....*....|....*....|....
gi 15599169  748 TAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:PRK11083  82 TARSDEVDRLVGLEIGADDYVAKP 105
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
670-779 2.43e-14

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 69.62  E-value: 2.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI---SNVPIIFISS 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQT 779
Cdd:cd18159  78 RDDNMDQVMAINMGGDDYITKPFDLDVLLA 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
670-771 2.69e-14

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 70.06  E-value: 2.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALT 748
Cdd:cd19923   3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                        90       100
                ....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19923  83 AEAKKENVIAAAQAGVNNYIVKP 105
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
697-783 2.79e-14

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 69.87  E-value: 2.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 697 ADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALtahshSGD-----RERCLAAGMSDYMAKP 771
Cdd:cd17593  31 AENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ--LETKVIVV-----SGDvqpeaKERVLELGALAFLKKP 103
                        90
                ....*....|..
gi 15599169 772 VKFEELQTLLHD 783
Cdd:cd17593 104 FDPEKLAQLLEE 115
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
670-777 3.92e-14

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 69.36  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRV-RTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRalpGCAELPVLALT 748
Cdd:cd19932   3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT---SENIAPIVLLT 79
                        90       100
                ....*....|....*....|....*....
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd19932  80 AYSQQDLVERAKEAGAMAYLVKPFSESDL 108
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
670-778 3.94e-14

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 69.23  E-value: 3.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALTA 749
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRS--EGRATPVLILTA 78
                        90       100
                ....*....|....*....|....*....
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd19934  79 RDSWQDKVEGLDAGADDYLTKPFHIEELL 107
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
670-777 4.32e-14

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 68.95  E-value: 4.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd17619   3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVTG 79
                        90       100
                ....*....|....*....|....*...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17619  80 RDDEVDRIVGLEIGADDYVTKPFNPREL 107
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
407-631 8.89e-14

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 73.46  E-value: 8.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  407 ALNQELAN-SNRLKDE--FLATVTHELRTPMSGVIGSLELM-QTVPMDVelaeyqrtAAGSAR--DMMRMVNDILALI-- 478
Cdd:PRK10755 122 ALNQLVSRlTSTLDQErlFTADVAHELRTPLAGIRLHLELLeKQHHIDV--------APLIARldQMMHTVEQLLQLAra 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  479 --ELQAGkLYprrEPFSL-RGLFDSLRAQYAPRVEEKGLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIKFTARGSv 555
Cdd:PRK10755 194 gqSFSSG-HY---QTVKLlEDVILPSQDELSEMLEQRQQTLLLPESAADI-TVQGDATLLRLLLRNLVENAHRYSPEGS- 267
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599169  556 TLRVAAGRTHDGvaLRVEVIDTGIGFDMAAGSDLYQRFVQADSsltrGYGGLGIGLALCRKLVELLGGELTHESRP 631
Cdd:PRK10755 268 TITIKLSQEDGG--AVLAVEDEGPGIDESKCGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHGQFFLQNRQ 337
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
669-781 1.55e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 73.73  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVED-NAINQLVTrGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLAL 747
Cdd:PRK11361   6 RILIVDDeDNVRRMLS-TAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHE--TRTPVILM 82
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599169  748 TAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:PRK11361  83 TAYAEVETAVEALRCGAFDYVIKPFDLDELNLIV 116
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
419-483 1.62e-13

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 65.70  E-value: 1.62e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599169   419 KDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAG 483
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
419-483 2.29e-13

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 65.28  E-value: 2.29e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599169    419 KDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAG 483
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
670-771 2.82e-13

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 66.63  E-value: 2.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLL---------DCQMPVMDGFATCRAIRALPGCA 740
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNDLskeldliitDIEMPKMDGYELTFELRDDPRLA 80
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 741 ELPVLALTAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19924  81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
527-641 3.04e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 66.66  E-value: 3.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 527 TLEGDAGKLAQALGYLVDNAIKFTARGS-VTLRVAAgrtHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSsltRGYG 605
Cdd:cd16940   6 QVQGDALLLFLLLRNLVDNAVRYSPQGSrVEIKLSA---DDGAVIRVE--DNGPGIDEEELEALFERFYRSDG---QNYG 77
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599169 606 GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16940  78 GSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
670-782 3.83e-13

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 66.74  E-value: 3.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELD--PDLPVILITG 78
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599169 750 HshsGDRERCLAA---GMSDYMAKPVKFEELQTLLH 782
Cdd:cd17549  79 H---GDVPMAVEAmraGAYDFLEKPFDPERLLDVVR 111
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
670-777 3.97e-13

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 66.63  E-value: 3.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd19939   2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREH---SHVPILMLTA 78
                        90       100
                ....*....|....*....|....*...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd19939  79 RTEEMDRVLGLEMGADDYLCKPFSPREL 106
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
670-771 4.22e-13

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 65.86  E-value: 4.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19927  81 KGMTSDRIKGYNAGCDGYLSKP 102
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
669-781 4.92e-13

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 69.46  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKL-GYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLA 746
Cdd:COG3279   3 KILIVDDEPLARERLERLLEKYpDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELD--PPPPIIF 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599169 747 LTAHShsgdrERCLAA---GMSDYMAKPVKFEELQTLL 781
Cdd:COG3279  81 TTAYD-----EYALEAfevNAVDYLLKPIDEERLAKAL 113
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
344-641 4.98e-13

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 72.85  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   344 LLGGIVnTLMVLGYLPnmfLTMYASQIGSalEVGLLS----LALADR---INAMKEERARI-LQESSRKLEALNQELANS 415
Cdd:TIGR03785 408 LFNVIL-AIMSIGTLA---LFGFASWISW--RIRRLSddaeAAIDSQgriSGAIPASRSRDeIGDLSRSFAQMVARLRQY 481
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   416 NRLKDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEY-QRTAAGSARdMMRMVNDILALIELQAGKLYPRREPFSL 494
Cdd:TIGR03785 482 THYLENMSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYlERAREGTER-LSMILNNMSEATRLEQAIQSAEVEDFDL 560
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   495 RGLFDSLRAQYAPRVEEKglRFALQLDDSlPDTLEGDAGKLAQALGYLVDNAIKFT-ARGSVTLRVAAgrtHDGVALrVE 573
Cdd:TIGR03785 561 SEVLSGCMQGYQMTYPPQ--RFELNIPET-PLVMRGSPELIAQMLDKLVDNAREFSpEDGLIEVGLSQ---NKSHAL-LT 633
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599169   574 VIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRP-GQGSRFLLRL 641
Cdd:TIGR03785 634 VSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISL 702
ompR PRK09468
osmolarity response regulator; Provisional
666-777 5.74e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 69.23  E-value: 5.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  666 EECTVLVVEDNA-INQLVTRgMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPV 744
Cdd:PRK09468   4 ENYKILVVDDDMrLRALLER-YLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRS--QNNPTPI 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 15599169  745 LALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK09468  81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPREL 113
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
670-782 1.15e-12

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 65.21  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNA-INQLVTrGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAL-PgcaELPVLAL 747
Cdd:cd17550   1 ILIVDDEEdIRESLS-GILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKyP---DLPVIMI 76
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599169 748 TAHshsGDRERCLAA---GMSDYMAKPVKFEELQTLLH 782
Cdd:cd17550  77 SGH---GTIETAVKAtklGAYDFIEKPLSLDRLLLTIE 111
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
669-777 1.79e-12

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 64.61  E-value: 1.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAElpVLAL 747
Cdd:cd17542   2 KVLIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMC 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 748 TAhshSGDRE---RCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17542  80 SA---MGQEEmvkEAIKAGAKDFIVKPFQPERV 109
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
669-771 2.26e-12

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 64.32  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcaELPVLALT 748
Cdd:cd19938   1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS---DVPIIMVT 77
                        90       100
                ....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19938  78 ARVEEIDRLLGLELGADDYICKP 100
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
531-641 2.26e-12

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 64.05  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAIKFTARGS-VTLRVAAGRTHdgvALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGI 609
Cdd:cd16925   1 DAEKYERVVLNLLSNAFKFTPDGGrIRCILEKFRLN---RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599169 610 GLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16925  78 GLSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
670-773 3.19e-12

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 63.94  E-value: 3.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd17622   3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK---YQGPILLLTA 79
                        90       100
                ....*....|....*....|....
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVK 773
Cdd:cd17622  80 LDSDIDHILGLELGADDYVVKPVE 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
416-477 3.53e-12

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 61.84  E-value: 3.53e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599169 416 NRLKDEFLATVTHELRTPMSGVIGSLELMQ-TVPMDVELAEYQRTAAGSARDMMRMVNDILAL 477
Cdd:cd00082   1 LQAKGEFLANVSHELRTPLTAIRGALELLEeELLDDEEQREYLERIREEAERLLRLINDLLDL 63
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
669-783 4.02e-12

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 65.32  E-value: 4.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgCAELPVLALT 748
Cdd:COG4567   6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRER--DPDARIVVLT 83
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHD 783
Cdd:COG4567  84 GYASIATAVEAIKLGADDYLAKPADADDLLAALER 118
PRK13557 PRK13557
histidine kinase; Provisional
402-777 4.21e-12

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 69.31  E-value: 4.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  402 SRKLEALNQelansnrlkdeFLATVTHELRTPMSGVIGSLELMQTV----PMDVEL----AEYQRTAAGSArdmMRMVND 473
Cdd:PRK13557 157 AQKMEALGQ-----------LTGGIAHDFNNLLQVMSGYLDVIQAAlshpDADRGRmarsVENIRAAAERA---ATLTQQ 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  474 ILALIELQagKLYPRrePFSLRGLFDSLrAQYAPRVEEKGLRFALQLDDSLPDTlEGDAGKLAQALGYLVDNAIKFTA-R 552
Cdd:PRK13557 223 LLAFARKQ--RLEGR--VLNLNGLVSGM-GELAERTLGDAVTIETDLAPDLWNC-RIDPTQAEVALLNVLINARDAMPeG 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  553 GSVTLR-----------VAAGRTHDGVALRVEVIDTGIGfdMAagSDLYQRfVQADSSLTRGYG-GLGIGLALCRKLVEL 620
Cdd:PRK13557 297 GRVTIRtrnveiededlAMYHGLPPGRYVSIAVTDTGSG--MP--PEILAR-VMDPFFTTKEEGkGTGLGLSMVYGFAKQ 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  621 LGGELTHESRPGQGSRfllrLQLTQPA--QGLAPPPRRAGgQAVRRPEECTVLVVEDNAINQLVTRGMLLKLGYRVRTAD 698
Cdd:PRK13557 372 SGGAVRIYSEVGEGTT----VRLYFPAsdQAENPEQEPKA-RAIDRGGTETILIVDDRPDVAELARMILEDFGYRTLVAS 446
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  699 NGSEALELLARE-RPDGVLLDCQMP-VMDGFATCR-AIRALPGcaeLPVLALTAHSHSGdRERCLAAGMS-DYMAKPVKF 774
Cdd:PRK13557 447 NGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAReARRRQPK---IKVLLTTGYAEAS-IERTDAGGSEfDILNKPYRR 522

                 ...
gi 15599169  775 EEL 777
Cdd:PRK13557 523 AEL 525
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-637 4.33e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 63.38  E-value: 4.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTaRGSVTLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALC 614
Cdd:cd16952   1 LRSAFSNLVSNAVKYT-PPSDTITVRWSQEESGARLSVE--DTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIV 77
                        90       100
                ....*....|....*....|...
gi 15599169 615 RKLVELLGGELTHESRPGQGSRF 637
Cdd:cd16952  78 KHVMSRHDARLLIASELGKGSRF 100
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-637 4.41e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 63.18  E-value: 4.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARGSVTLRVAAGRT--HDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSltrgygGLGIGLA 612
Cdd:cd16920   1 IQQVLINLVRNGIEAMSEGGCERRELTIRTspADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGLS 74
                        90       100
                ....*....|....*....|....*
gi 15599169 613 LCRKLVELLGGELTHESRPGQGSRF 637
Cdd:cd16920  75 ICRSIIEAHGGRLSVESPAGGGATF 99
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
378-641 8.09e-12

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 68.27  E-value: 8.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  378 LLSLALADRINAMKEERARilqESSRKLEAlnqELANSNRLK--DEFLATVTHELRTPMSGVIG-SLELMQTVPMDVELA 454
Cdd:PRK10364 200 LATVLLASLLAFFWYRRYL---RSRQLLQD---EMKRKEKLValGHLAAGVAHEIRNPLSSIKGlAKYFAERAPAGGEAH 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  455 EYQRTAAGSARDMMRMVNDILALIE-----LQAGKLYPRREpFSLRglfdsLRAQYAprvEEKGLRFALQLDDSLPdTLE 529
Cdd:PRK10364 274 QLAQVMAKEADRLNRVVSELLELVKpthlaLQAVDLNDLIN-HSLQ-----LVSQDA---NSREIQLRFTANDTLP-EIQ 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  530 GDAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviDTGIGFdmaAGSDLYQRFvqaDSSLTRGYGGLGI 609
Cdd:PRK10364 344 ADPDRLTQVLLNLYLNAIQAIGQHG-VISVTASESGAGVKISVT--DSGKGI---AADQLEAIF---TPYFTTKAEGTGL 414
                        250       260       270
                 ....*....|....*....|....*....|..
gi 15599169  610 GLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:PRK10364 415 GLAVVHNIVEQHGGTIQVASQEGKGATFTLWL 446
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
669-771 8.22e-12

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 62.68  E-value: 8.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRA-LPgcaELPVLAL 747
Cdd:cd19919   2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQrHP---DLPVIIM 78
                        90       100
                ....*....|....*....|....*..
gi 15599169 748 TAHShsgDRERCLAA---GMSDYMAKP 771
Cdd:cd19919  79 TAHS---DLDSAVSAyqgGAFEYLPKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
671-771 1.05e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 62.68  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  671 LVVEDNAINQLVTRGMLLKLGYR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:PRK10610   9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTA 88
                         90       100
                 ....*....|....*....|..
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:PRK10610  89 EAKKENIIAAAQAGASGYVVKP 110
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
669-784 2.01e-11

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 61.49  E-value: 2.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKL-GYRV-RTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlPGCaELPVLA 746
Cdd:cd19925   2 NVLIVEDDPMVAEIHRAYVEQVpGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA-AGH-DVDVIV 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDW 784
Cdd:cd19925  80 VTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
669-777 2.73e-11

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 61.31  E-value: 2.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpgCAELPVLALT 748
Cdd:cd17594   1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA---RSDVPIIIIS 77
                        90       100       110
                ....*....|....*....|....*....|
gi 15599169 749 AHS-HSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd17594  78 GDRrDEIDRVVGLELGADDYLAKPFGLREL 107
PRK10766 PRK10766
two-component system response regulator TorR;
669-777 3.57e-11

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 63.52  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALT 748
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSR---STVGIILVT 80
                         90       100
                 ....*....|....*....|....*....
gi 15599169  749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELREL 109
PRK11517 PRK11517
DNA-binding response regulator HprR;
670-777 3.79e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 63.76  E-value: 3.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpgCAELPVLALTA 749
Cdd:PRK11517   3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRT---AKQTPVICLTA 79
                         90       100
                 ....*....|....*....|....*...
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK11517  80 RDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
670-771 3.86e-11

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 60.15  E-value: 3.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAiNQLVTRGMLLKL-GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALT 748
Cdd:cd19936   1 IALVDDDR-NILTSVSMALEAeGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLT 76
                        90       100
                ....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19936  77 SKDDEIDEVFGLRMGADDYITKP 99
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
670-771 5.35e-11

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 60.07  E-value: 5.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:cd17602   1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17602  81 KDGLVDRIRAKMAGASGYLTKP 102
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
670-771 5.47e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 64.79  E-value: 5.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNA-INQLVTRgML-----LKLgyrVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAL-PgcaeL 742
Cdd:PRK00742   6 VLVVDDSAfMRRLISE-ILnsdpdIEV---VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLrP----T 77
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15599169  743 PVL---ALTahsHSGDRE--RCLAAGMSDYMAKP 771
Cdd:PRK00742  78 PVVmvsSLT---ERGAEItlRALELGAVDFVTKP 108
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-641 6.39e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 59.61  E-value: 6.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTAR-GSVTLRVAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQadsslTRGYGGLGIGLAL 613
Cdd:cd16915   1 LITIVGNLIDNALDALAAtGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFERGVS-----TKGQGERGIGLAL 75
                        90       100
                ....*....|....*....|....*...
gi 15599169 614 CRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16915  76 VRQSVERLGGSITVESEPGGGTTFSIRI 103
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
670-771 7.64e-11

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 59.52  E-value: 7.64e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:cd17621   1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR---SNVPVIMVTA 77
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17621  78 KDSEIDKVVGLELGADDYVTKP 99
PRK15115 PRK15115
response regulator GlrR; Provisional
670-794 8.33e-11

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 64.86  E-value: 8.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVtrGM-LLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAI-RALPGcaeLPVLAL 747
Cdd:PRK15115   9 LLVDDDPGLLKLL--GMrLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIqKVQPG---MPVIIL 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15599169  748 TAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLHDWL----------LCQPIVTKS 794
Cdd:PRK15115  84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALeqsapatderWREAIVTRS 140
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
670-779 9.25e-11

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 59.90  E-value: 9.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAI--RALPgcaeLPVLAL 747
Cdd:cd17572   1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIqeRSLP----TSVIVI 76
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599169 748 TAHShSGDrercLA-----AGMSDYMAKPVKFEELQT 779
Cdd:cd17572  77 TAHG-SVD----IAveamrLGAYDFLEKPFDADRLRV 108
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
670-782 9.68e-11

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 59.73  E-value: 9.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAK--VKTPILILSG 78
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLLH 782
Cdd:cd17616  79 LADIEDKVKGLGFGADDYMTKPFHKDELVARIH 111
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
669-777 1.22e-10

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 61.65  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALT 748
Cdd:COG4566   1 TVYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARG--SPLPVIFLT 78
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599169 749 AHshsGDRERCLAA---GMSDYMAKPVKFEEL 777
Cdd:COG4566  79 GH---GDVPMAVRAmkaGAVDFLEKPFDDQAL 107
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-647 1.29e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 58.88  E-value: 1.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARgsvTLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALC 614
Cdd:cd16949   1 LARALENVLRNALRYSPS---KILLDISQDGDQWTITIT--DDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIA 75
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 615 RKLVELLGGELTHESRPGQGsrflLRLQLTQPA 647
Cdd:cd16949  76 ERAIEQHGGKIKASNRKPGG----LRVRIWLPA 104
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
421-649 1.95e-10

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 64.22  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  421 EFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTaagsardMMRMVNDILALIE--LQAGKlyPRR---EPFSLR 495
Cdd:PRK11360 392 ELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSV-------VLREVDRLNKVIDqlLEFSR--PREsqwQPVSLN 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  496 GLFDSLrAQYAPRVEEK-GLRFALQLDDSLPdTLEGDAGKLAQALGYLVDNAIK-FTARGSVTLRVaaGRTHDGvALRVE 573
Cdd:PRK11360 463 ALVEEV-LQLFQTAGVQaRVDFETELDNELP-PIWADPELLKQVLLNILINAVQaISARGKIRIRT--WQYSDG-QVAVS 537
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599169  574 VIDTGIGFDMAAGSDLYQRFVQADSSltrgygGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLTQPAQG 649
Cdd:PRK11360 538 IEDNGCGIDPELLKKIFDPFFTTKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGNQ 607
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-634 4.54e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 57.07  E-value: 4.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFtarGSVTLRVAAGrtHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSltRGYGGLGIGLALC 614
Cdd:cd16950   1 LKRVLSNLVDNALRY---GGGWVEVSSD--GEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIV 73
                        90       100
                ....*....|....*....|
gi 15599169 615 RKLVELLGGELTHESRPGQG 634
Cdd:cd16950  74 QRISDAHGGSLTLANRAGGG 93
PRK10816 PRK10816
two-component system response regulator PhoP;
670-781 4.72e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 60.52  E-value: 4.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALTA 749
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS--NDVSLPILVLTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEE----LQTLL 781
Cdd:PRK10816  81 RESWQDKVEVLSAGADDYVTKPFHIEEvmarMQALM 116
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
508-641 5.57e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 62.62  E-value: 5.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  508 RVEEKGLRFALQLDDSLPDTL-EGDAGKLAQALGYLVDNAI-----KFTARGSVTLRVAAGRTHdgvalrVEVIDTGIGF 581
Cdd:PRK11086 406 RARELGITLIISEDSQLPDSGdEDQVHELITILGNLIENALeavggEEGGEISVSLHYRNGWLH------CEVSDDGPGI 479
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  582 DMAAGSDLYQRFVQadsslTRGyGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:PRK11086 480 APDEIDAIFDKGYS-----TKG-SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533
PRK10643 PRK10643
two-component system response regulator PmrA;
670-778 7.47e-10

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 59.66  E-value: 7.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAinqLVTRGMLLKL---GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlPGCaELPVLA 746
Cdd:PRK10643   3 ILIVEDDT---LLLQGLILALqteGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ-KKY-TLPVLI 77
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15599169  747 LTAHSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:PRK10643  78 LTARDTLEDRVAGLDVGADDYLVKPFALEELH 109
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
670-772 8.06e-10

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 56.59  E-value: 8.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARE-RPDGVLLDCQMP-VMDGFATCRAIRAL-PGcaeLPVLA 746
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEARRRrPD---LKVLL 77
                        90       100
                ....*....|....*....|....*.
gi 15599169 747 LTAHSHSGDRERCLAAGMsDYMAKPV 772
Cdd:cd18161  78 TSGYAENAIEGGDLAPGV-DVLSKPF 102
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
665-771 9.04e-10

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 59.70  E-value: 9.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 PEECTVLVVEDN-AINQLVTrGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELP 743
Cdd:PRK10710   8 ENTPRILIVEDEpKLGQLLI-DYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRF---SDIP 83
                         90       100
                 ....*....|....*....|....*...
gi 15599169  744 VLALTAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:PRK10710  84 IVMVTAKIEEIDRLLGLEIGADDYICKP 111
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
665-782 9.70e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 59.27  E-value: 9.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  665 PEECTVLVVED-----NAINQLVTRGMLLKLgyrVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpgc 739
Cdd:PRK10651   4 QEPATILLIDDhpmlrTGVKQLISMAPDITV---VGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15599169  740 AELP--VLALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLH 782
Cdd:PRK10651  77 KSLSgrIVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQ 121
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
670-777 1.09e-09

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 56.51  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDN-----AINQLVTRGMLLKLgyrVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRA-LPGCAelp 743
Cdd:cd19930   1 VLIAEDQemvrgALAALLELEDDLEV---VAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREeLPDTK--- 74
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599169 744 VLALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:cd19930  75 VLIVTTFGRPGYFRRALAAGVDGYVLKDRPIEEL 108
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-643 1.18e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 56.28  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARgsvTLRVAAgrTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALC 614
Cdd:cd16939   1 MARALDNLLRNALRYAHR---TVRIAL--LVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIV 75
                        90       100
                ....*....|....*....|....*....
gi 15599169 615 RKLVELLGGELTHESRPGQGSRFLLRLQL 643
Cdd:cd16939  76 HRVALWHGGHVECDDSELGGACFRLTWPR 104
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
669-771 1.22e-09

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 55.97  E-value: 1.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERP-DGVLLDCQMPVMDGFATCRAIRALPgcAELPVLAL 747
Cdd:cd18160   1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKID--PDVKILFI 78
                        90       100
                ....*....|....*....|....
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd18160  79 SGGAAAAPELLSDAVGDNATLKKP 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
332-646 1.41e-09

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 59.63  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 332 VARYFIIAWTAFLLGGIVNTLMVLgylpnmfLTMYASQIGSALEvgLLSLALADRINAMKEERARILQEssrklealnqe 411
Cdd:COG4585   1 LLALALLGALALLVGALLGLLLAL-------VLLRARRAERAAE--LERELAARAEEAREEERRRIARE----------- 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 412 lansnrLKDeflaTVTHELrtpmSGVIGSLE-LMQTVPMDVE-LAEYQRTAAGSARDMMRMVNDILALIelqagklypRR 489
Cdd:COG4585  61 ------LHD----GVGQSL----SAIKLQLEaARRLLDADPEaAREELEEIRELAREALAELRRLVRGL---------RP 117
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 490 EPFSLRGLFDSLRAQYAPRVEEKGLRFALQLD---DSLPDTLEGDAGKLAQALgylVDNAIKfTARGS---VTLRVAAGR 563
Cdd:COG4585 118 PALDDLGLAAALEELAERLLRAAGIRVELDVDgdpDRLPPEVELALYRIVQEA---LTNALK-HAGATrvtVTLEVDDGE 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 564 thdgvaLRVEVIDTGIGFDMAAGSdlyqrfvqadssltrgygGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQL 643
Cdd:COG4585 194 ------LTLTVRDDGVGFDPEAAP------------------GGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPL 249

                ...
gi 15599169 644 TQP 646
Cdd:COG4585 250 AAA 252
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
669-765 1.46e-09

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 56.82  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAinqLVTRGMLLKL----GYRV-RTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIralpgcaelp 743
Cdd:COG2197   3 RVLIVDDHP---LVREGLRALLeaepDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL---------- 69
                        90       100
                ....*....|....*....|....*.
gi 15599169 744 vlaLTahshsgDRE----RCLAAGMS 765
Cdd:COG2197  70 ---LT------PRErevlRLLAEGLS 86
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-638 3.62e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 54.77  E-value: 3.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVqadsSLTRGYGG---L 607
Cdd:cd16945   1 DPFLLRQAINNLLDNAIDFSPEGG-LIALQLEADTEGIELLVF--DEGSGIPDYALNRVFERFY----SLPRPHSGqksT 73
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 608 GIGLALCRKLVELLGGELTHESRPGQGSRFL 638
Cdd:cd16945  74 GLGLAFVQEVAQLHGGRITLRNRPDGVLAFL 104
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
494-641 3.62e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 55.72  E-value: 3.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 494 LRGLFDSLRAQYAprveEKGLRFALQLDDSLpdTLEGDAGKLAQALGYLVDNAIKFTARgsvTLRVAAGRTHDGVALRVE 573
Cdd:cd16954   3 LDSLCSALNKVYQ----RKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWCLE---FVEVTARQTDGGLHLIVD 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599169 574 viDTGIGFDMAAGSDLYQRFVQADSSLTrgygGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16954  74 --DDGPGVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
519-642 4.11e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 55.21  E-value: 4.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 519 QLDDSLPDT---LEGDAGKLAQALGYLVDNAIKFTARG---SVTLRvaagrtHDGVALRVEVIDTGIGFDMAAGSDLYQR 592
Cdd:cd16947   2 QVEINIPDRpiyANANTEALQRILKNLISNAIKYGSDGkflGMTLR------EDEKHVYIDIWDKGKGISETEKDHVFER 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15599169 593 FVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQ 642
Cdd:cd16947  76 LYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTLK 125
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
524-641 4.57e-09

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 55.54  E-value: 4.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 524 LPDTLEGDAGKLAQALGYLVDNAIKFTAR-GSVTLRVAAGRTHDG-------------------VALRVEVIDTGIGFDM 583
Cdd:cd16938   1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLEGGSEDrsdrdwgpwrpsmsdesveIRFEVEINDSGSPSIE 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599169 584 AAGSDlyqrfvqadSSLTRGYG----GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16938  81 SASMR---------NSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
670-778 6.07e-09

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 54.48  E-value: 6.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID--ENIRVIIMTA 80
                        90       100
                ....*....|....*....|....*....
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17553  81 YGELDMIQESKELGALTHFAKPFDIDEIR 109
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
670-771 6.37e-09

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 54.15  E-value: 6.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDN-AINQLVTRGMLLKLGYRV-RTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLAL 747
Cdd:cd17561   4 VLIADDNrEFVQLLEEYLNSQPDMEVvGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIML 83
                        90       100
                ....*....|....*....|....
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17561  84 TAFGQEDITQRAVELGASYYILKP 107
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
410-644 6.59e-09

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 58.97  E-value: 6.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 410 QELANSNRLK--DEFLATVTHELRTPMSGVIGSLELMQTVP------MDVELAEYQRtaagsardMMRMVNDILALIELQ 481
Cdd:COG5805 276 ELMARSEKLSiaGQLAAGIAHEIRNPLTSIKGFLQLLQPGIedkeeyFDIMLSELDR--------IESIISEFLALAKPQ 347
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 482 AgklyPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSLPDtLEGDAGKLAQALGYLVDNAIK-FTARGSVTLRVA 560
Cdd:COG5805 348 A----VNKEKENINELIQDVVTLLETEAILHNIQIRLELLDEDPF-IYCDENQIKQVFINLIKNAIEaMPNGGTITIHTE 422
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 561 AGrtHDGVALRveVIDTGIGFDMAAGSDLYQRFvqadssLTRGYGGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLR 640
Cdd:COG5805 423 EE--DNSVIIR--VIDEGIGIPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492

                ....
gi 15599169 641 LQLT 644
Cdd:COG5805 493 LPLS 496
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
670-771 7.45e-09

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 53.94  E-value: 7.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVE-DNAINQLVTRgMLLKLGYRVRTADNGSEALELLARERP--DGVLLDCQMPVMDGFATCRAIRALPGCAELPVLA 746
Cdd:cd17582   1 VLLVEnDDSTRQIVTA-LLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIM 79
                        90       100
                ....*....|....*....|....*
gi 15599169 747 LTAHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd17582  80 MSSQDSVGVVFKCLSKGAADYLVKP 104
PRK10693 PRK10693
two-component system response regulator RssB;
697-773 7.60e-09

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 57.69  E-value: 7.60e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599169  697 ADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRaLPGcAELPVLALTAHSHSGDRERCLAAGMSDYMAKPVK 773
Cdd:PRK10693   3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR-NRG-DQTPVLVISATENMADIAKALRLGVQDVLLKPVK 77
PRK15479 PRK15479
transcriptional regulator TctD;
670-781 7.91e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 56.65  E-value: 7.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPgcAELPVLALTA 749
Cdd:PRK15479   3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRG--QTLPVLLLTA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:PRK15479  81 RSAVADRVKGLNVGADDYLPKPFELEELDARL 112
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-643 1.28e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 53.19  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIK-FTARGSVTLRVAAgrTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQadsslTRGYG-GLGIGLA 612
Cdd:cd16943   4 LNQVLLNLLVNAAQaMEGRGRITIRTWA--HVDQVLIEVE--DTGSGIDPEILGRIFDPFFT-----TKPVGeGTGLGLS 74
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 613 LCRKLVELLGGELTHESRPGQGSRFLLRLQL 643
Cdd:cd16943  75 LSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
669-778 1.89e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 55.58  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVED-NAINQLVtRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFatcRAIRALPGCAELPVLAL 747
Cdd:PRK10529   3 NVLIVEDeQAIRRFL-RTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGI---EFIRDLRQWSAIPVIVL 78
                         90       100       110
                 ....*....|....*....|....*....|.
gi 15599169  748 TAHSHSGDRERCLAAGMSDYMAKPVKFEELQ 778
Cdd:PRK10529  79 SARSEESDKIAALDAGADDYLSKPFGIGELQ 109
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
670-771 2.34e-08

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 52.54  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALTA 749
Cdd:cd19926   1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQ--RLPQTPVAVITA 78
                        90       100
                ....*....|....*....|..
gi 15599169 750 HSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19926  79 YGSLDTAIEALKAGAFDFLTKP 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
669-726 2.43e-08

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 52.79  E-value: 2.43e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVED--NAINQLvtRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDG 726
Cdd:cd17569   2 TILLVDDepNILKAL--KRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDG 59
PLN03029 PLN03029
type-a response regulator protein; Provisional
670-780 3.36e-08

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 55.04  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLA-----RERPDG---------------VLLDCQMPVMDGFAT 729
Cdd:PLN03029  11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddRSNPDTpsvspnshqevevnlIITDYCMPGMTGYDL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15599169  730 CRAIRALPGCAELPVLALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTL 780
Cdd:PLN03029  91 LKKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDLNRL 141
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
669-778 3.42e-08

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 52.21  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpGCAeLPVLALT 748
Cdd:cd17537   2 TVYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR-GSN-IPIIFIT 79
                        90       100       110
                ....*....|....*....|....*....|...
gi 15599169 749 AHshsGDRE---RCLAAGMSDYMAKPVKFEELQ 778
Cdd:cd17537  80 GH---GDVPmavEAMKAGAVDFLEKPFRDQVLL 109
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
670-782 8.44e-08

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 55.65  E-value: 8.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALTA 749
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQ--RHPMLPVIIMTA 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15599169  750 HShsgDRERCLAA---GMSDYMAKPVKFEELQTLLH 782
Cdd:PRK10923  84 HS---DLDAAVSAyqqGAFDYLPKPFDIDEAVALVE 116
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-641 9.14e-08

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.03  E-value: 9.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARGSVTLRVAAGRThdGVALRVEVIDTGIGFDMAAGSDLYQRFVqADSSLTRGYG-GLGIGLAL 613
Cdd:cd16953   1 LGQVLRNLIGNAISFSPPDTGRITVSAMPT--GKMVTISVEDEGPGIPQEKLESIFDRFY-TERPANEAFGqHSGLGLSI 77
                        90       100       110
                ....*....|....*....|....*....|..
gi 15599169 614 CRKLVELLGGELTHESR--PGQ--GSRFLLRL 641
Cdd:cd16953  78 SRQIIEAHGGISVAENHnqPGQviGARFTVQL 109
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
670-782 1.07e-07

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 50.81  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVED-----NAINQLVTRGMLLKLgyrVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAElpV 744
Cdd:cd19931   1 VLLIDDhpllrKGIKQLIELDPDFTV---VGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSAR--I 75
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15599169 745 LALTAHSHSGDRERCLAAGMSDYMAKPVKFEELQTLLH 782
Cdd:cd19931  76 VILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
670-777 1.29e-07

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 53.18  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALTA 749
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                         90       100
                 ....*....|....*....|....*...
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK10161  85 RGEEEDRVRGLETGADDYITKPFSPKEL 112
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
424-641 1.32e-07

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 54.23  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  424 ATVTHELRTPMSGVIGSLE------------LMQTVPMDVE----LAEYQRTaagsardmmrmvndiLALIELQAGKLyp 487
Cdd:NF012226 143 AAIAHELRTPITILQGRLQgildgvfepdpaLFKSLLNQVEglshLVEDLRT---------------LSLVENQQLRL-- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  488 RREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDslpDTLEGDAGKLAQALGYLVDNAIKFTARGsvTLRVAAGRTHDG 567
Cdd:NF012226 206 NYESVDLKDSIEKVLKMFEDRLEQAQLTIVLNLTA---TPVFCDRRRIEQVLIALIDNAIRYANAG--KLKISSSVIQDD 280
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599169  568 VALRVEviDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLALCRKLVELLGGELTHeSRPGQGSRFLLRL 641
Cdd:NF012226 281 WILQIE--DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEY-SNSQGNSVFTIKL 351
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
668-772 2.04e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 53.73  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  668 CTVLVVEDNA-INQLVTRGMLLKLGYRVR-TADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVL 745
Cdd:PRK12555   1 MRIGIVNDSPlAVEALRRALARDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERPCPILIVT 80
                         90       100
                 ....*....|....*....|....*..
gi 15599169  746 ALTAhSHSGDRERCLAAGMSDYMAKPV 772
Cdd:PRK12555  81 SLTE-RNASRVFEAMGAGALDAVDTPT 106
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
694-781 2.27e-07

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 50.23  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 694 VRTADNGSEALELLARERPDGVLLDCQMPVMDGFatcRAIRALPGCAELP-VLALTAHshsgdRERCLAA---GMSDYMA 769
Cdd:cd17532  27 VGEAENGEEALEAIEELKPDVVFLDIQMPGLDGL---ELAKKLSKLAKPPlIVFVTAY-----DEYAVEAfelNAVDYLL 98
                        90
                ....*....|..
gi 15599169 770 KPVKFEELQTLL 781
Cdd:cd17532  99 KPFSEERLAEAL 110
PRK10604 PRK10604
sensor protein RstB; Provisional
525-657 2.29e-07

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 53.84  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  525 PDTLEGDAGKLAQALGYLVDNAIKFTARgsvtlRVAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGY 604
Cdd:PRK10604 310 GDYGALDMRLMERVLDNLLNNALRYAHS-----RVRVSLLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRAT 384
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599169  605 GGLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLqltqPAQGLAPPPRRA 657
Cdd:PRK10604 385 GGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSW----PVWHNLPQFTSA 433
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
670-777 3.79e-07

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 51.73  E-value: 3.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLaRERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVLALTA 749
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLTA 79
                         90       100
                 ....*....|....*....|....*...
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK10955  80 RGSELDRVLGLELGADDYLPKPFNDREL 107
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-641 4.40e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 49.07  E-value: 4.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAI-----KFTARGSVTLRVAAGRTHDgvaLRVEVIDTGIGFDMAAGSDLYQRFVQADSSltrgyg 605
Cdd:cd16944   1 DTTQISQVLTNILKNAAeaiegRPSDVGEVRIRVEADQDGR---IVLIVCDNGKGFPREMRHRATEPYVTTRPK------ 71
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599169 606 GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16944  72 GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
669-748 9.47e-07

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 48.21  E-value: 9.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAI-NQLVTRGMLlKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgCAELPVLAL 747
Cdd:cd17563   2 SLLLVDDDEVfAERLARALE-RRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRAL--QPDARIVVL 78

                .
gi 15599169 748 T 748
Cdd:cd17563  79 T 79
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
545-641 1.17e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 47.16  E-value: 1.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 545 NAIKFTARGSVTLRVAagRTHDGVALRVEviDTGIGFDMAAGSDlyqrfvqadsslTRGYGGLGIglalcRKLVELLGGE 624
Cdd:cd16917  11 NALKHAGASRVRVTLS--YTADELTLTVV--DDGVGFDGPAPPG------------GGGFGLLGM-----RERAELLGGT 69
                        90
                ....*....|....*..
gi 15599169 625 LTHESRPGQGSRFLLRL 641
Cdd:cd16917  70 LTIGSRPGGGTRVTARL 86
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
670-781 1.49e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 49.92  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNA-INQLVTRGmLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlpGCAELPVLALT 748
Cdd:PRK09836   3 LLIVEDEKkTGEYLTKG-LTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRS--ANKGMPILLLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15599169  749 AHSHSGDRERCLAAGMSDYMAKPVKFEEL----QTLL 781
Cdd:PRK09836  80 ALGTIEHRVKGLELGADDYLVKPFAFAELlarvRTLL 116
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
690-735 2.14e-06

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 46.88  E-value: 2.14e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15599169 690 LGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRA 735
Cdd:cd17565  23 LGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKD 68
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-629 2.85e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 46.61  E-value: 2.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTARGSvTLRVAAGRTHDGValRVEVIDTGIGFDMAAGSDLYQRFVQADSSltRGYGGLGIGLALC 614
Cdd:cd16923   1 LQRVFSNLLSNAIKYSPENT-RIYITSFLTDDVV--NIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIA 75
                        90
                ....*....|....*
gi 15599169 615 RKLVELLGGELTHES 629
Cdd:cd16923  76 KAIIELHGGSASAEY 90
PRK10336 PRK10336
two-component system response regulator QseB;
670-781 4.17e-06

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 48.74  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAlPGCAElPVLALTA 749
Cdd:PRK10336   3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWRE-KGQRE-PVLILTA 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15599169  750 HSHSGDRERCLAAGMSDYMAKPVKFEELQTLL 781
Cdd:PRK10336  81 RDALAERVEGLRLGADDYLCKPFALIEVAARL 112
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
670-718 4.54e-06

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 46.10  E-value: 4.54e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGY-RVRTADNGSEALELLARERPDGVLLD 718
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCD 50
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-632 5.00e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 45.85  E-value: 5.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAIKFTAR--GSVTLR------VAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVqadsslTRGYGG 606
Cdd:cd16918   1 LIQVFLNLVRNAAQALAGsgGEIILRtrtqrqVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMV------SGRENG 74
                        90       100
                ....*....|....*....|....*.
gi 15599169 607 LGIGLALCRKLVELLGGELTHESRPG 632
Cdd:cd16918  75 TGLGLAIAQNIVSQHGGVIECDSQPG 100
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-637 6.20e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 45.74  E-value: 6.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAIKFTARGS-VTLRVAagrtHDGVALRVEVIDTGIGFDmaaGSDLYQRFvqaDSSLTrGYGG--- 606
Cdd:cd16948   2 DAKWLSFIIGQIVSNALKYSKQGGkIEIYSE----TNEQGVVLSIKDFGIGIP---EEDLPRVF---DKGFT-GENGrnf 70
                        90       100       110
                ....*....|....*....|....*....|....
gi 15599169 607 ---LGIGLALCRKLVELLGGELTHESRPGQGSRF 637
Cdd:cd16948  71 qesTGMGLYLVKKLCDKLGHKIDVESEVGEGTTF 104
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
669-733 7.10e-06

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 45.90  E-value: 7.10e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGY-RVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAI 733
Cdd:cd17530   2 RVLVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHL 67
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
669-771 1.50e-05

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 45.44  E-value: 1.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNaINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRAL-PgcaELPVLAL 747
Cdd:cd17596   2 TILVVDDE-VRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERwP---EVVRIII 77
                        90       100
                ....*....|....*....|....*
gi 15599169 748 TAHSHSGDRERCL-AAGMSDYMAKP 771
Cdd:cd17596  78 SGYTDSEDIIAGInEAGIYQYLTKP 102
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
669-775 2.74e-05

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 44.32  E-value: 2.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNA-INQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLAL 747
Cdd:cd17575   2 MVLLVDDQAiIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                        90       100
                ....*....|....*....|....*....
gi 15599169 748 TAHSHSGDRERCLAAGMSDYMAK-PVKFE 775
Cdd:cd17575  82 STKEEPEVKSEAFALGANDYLVKlPDKIE 110
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
279-648 2.81e-05

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 47.59  E-value: 2.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 279 RGLLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIFAAGILAWLRGMRVARYFIIAWTAFLLGGIVNTLMVLGYL 358
Cdd:COG3920 170 LRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARG 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 359 PNMFLTMYASQIGSALEVGLLSLALADRINAMKEERARiLQESSRKLEALNQELanSNRLKDEFlatvthelrtpmsGVI 438
Cdd:COG3920 250 LGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEE-LEASLEEKELLLREL--HHRVKNNL-------------QVV 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 439 GSLELMQTvpmdvelaeyQRTAAGSARDMMRMVND-ILALIELQaGKLY--PRREPFSLRGLFDSLRAQYAPRVEEKGLR 515
Cdd:COG3920 314 SSLLRLQA----------RRADDPEAREALEESQNrIQALALVH-ELLYqsEDWEGVDLRDYLRELLEPLRDSYGGRGIR 382
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 516 FALQLDDslpDTLEGDAgklAQALGY----LVDNAIK--FTARGSVTLRVAAGRTHDGvaLRVEVIDTGIGFDmaagsdl 589
Cdd:COG3920 383 IELDGPD---VELPADA---AVPLGLilneLVTNALKhaFLSGEGGRIRVSWRREDGR--LRLTVSDNGVGLP------- 447
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599169 590 yQRFVQADSSltrgygglGIGLALCRKLVELLGGELTHESRPgqGSRFLLRLQLTQPAQ 648
Cdd:COG3920 448 -EDVDPPARK--------GLGLRLIRALVRQLGGTLELDRPE--GTRVRITFPLAELAA 495
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
669-750 3.23e-05

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 43.78  E-value: 3.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 669 TVLVVEDNAINQLVTRGMLLKLGYRV----RTADngsEALELLARERPDGVLLDCQMPvmDGFATCRAIRALPGCAELPV 744
Cdd:cd17540   2 RVLIIEDEPLIAMDLEQIVEDLGHQVvgiaRTRD---EAVALARRERPDLILADIQLA--DGSSGIDAVNEILTTHDVPV 76

                ....*.
gi 15599169 745 LALTAH 750
Cdd:cd17540  77 IFVTAY 82
PRK15369 PRK15369
two component system response regulator;
670-770 3.51e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 45.84  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNA--INQLvtRGMLLKLG-YR-VRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRA-LPgcaELPV 744
Cdd:PRK15369   6 ILLVDDHEliINGI--KNMLAPYPrYKiVGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQrWP---AMNI 80
                         90       100
                 ....*....|....*....|....*.
gi 15599169  745 LALTAHSHSGDRERCLAAGMSDYMAK 770
Cdd:PRK15369  81 LVLTARQEEHMASRTLAAGALGYVLK 106
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
511-645 3.98e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 46.93  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 511 EKGLRFALQLDDSLPDTLEgdagkLAQALGYLVDNAIKF---TARGSVTLRVAAGRTHDgvALRVEVIDTGIGFDMAAGS 587
Cdd:COG2972 318 GDRLEVEIEIDEELLDLLI-----PKLILQPLVENAIEHgiePKEGGGTIRISIRKEGD--RLVITVEDNGVGMPEEKLE 390
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599169 588 DLYQRFVQADSsltrgygGLGIGLALCRKLVELLGGE---LTHESRPGQGSRFLLRLQLTQ 645
Cdd:COG2972 391 KLLEELSSKGE-------GRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLEE 444
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
406-612 4.79e-05

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 46.46  E-value: 4.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  406 EALNQELANSNRLkdefLATVTHELRTPmsgvigsLELMQtvpMDVELAeyqRTAAGSARDMMR----------MVNDIL 475
Cdd:PRK09470 234 TALERMMTSQQRL----LSDISHELRTP-------LTRLQ---LATALL---RRRQGESKELERieteaqrldsMINDLL 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  476 ALIELQAgKLYPRREPFSLRGLFDSL--RAQYAPRVEEKGLRFALQLDdslPDTLEGDAGKLAQALGYLVDNAIKFTARg 553
Cdd:PRK09470 297 VLSRNQQ-KNHLERETFKANSLWSEVleDAKFEAEQMGKSLTVSAPPG---PWPINGNPNALASALENIVRNALRYSHT- 371
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599169  554 svtlRVAAGRTHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGYGGLGIGLA 612
Cdd:PRK09470 372 ----KIEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLA 426
PRK11173 PRK11173
two-component response regulator; Provisional
670-777 5.05e-05

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 45.39  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDnainQLVTRGMLLKL----GYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALpgcAELPVL 745
Cdd:PRK11173   6 ILIVED----ELVTRNTLKSIfeaeGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQ---ANVALM 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 15599169  746 ALTAHSHSGDRERCLAAGMSDYMAKPVKFEEL 777
Cdd:PRK11173  79 FLTGRDNEVDKILGLEIGADDYITKPFNPREL 110
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
669-770 1.31e-04

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.24  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  669 TVLVVEDNA-INQLVTrGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRA-LPGcaelPVLA 746
Cdd:PRK10701   3 KIVFVEDDAeVGSLIA-AYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPkWQG----PIVL 77
                         90       100
                 ....*....|....*....|....*.
gi 15599169  747 LTahSHSGDRERCLA--AGMSDYMAK 770
Cdd:PRK10701  78 LT--SLDSDMNHILAleMGACDYILK 101
PRK10337 PRK10337
sensor protein QseC; Provisional
396-634 1.58e-04

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 45.03  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  396 RILQESSRKLEALNQELANSNRL---KDEFLATVTHELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSARD-MMRMV 471
Cdd:PRK10337 211 GVPSEVRPLVEALNQLFARTHAMmvrERRFTSDAAHELRSPLAALKVQTEVAQLSDDDPQARKKALLQLHAGIDrATRLV 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  472 NDILALIELQAGKLYPRREPFSLRGLFDSLRAQYAPRVEEKGLRFALQLDDSlPDTLEGDAGKLAQALGYLVDNAIKFTA 551
Cdd:PRK10337 291 DQLLTLSRLDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAH-PVIRTGQPLLLSLLVRNLLDNAIRYSP 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  552 RGS-VTLRVAAGRTHdgvalrveVIDTGIGFDMAAGSDLYQRFV----QADSsltrgygGLGIGLALCRKLVELLGGELT 626
Cdd:PRK10337 370 QGSvVDVTLNARNFT--------VRDNGPGVTPEALARIGERFYrppgQEAT-------GSGLGLSIVRRIAKLHGMNVS 434

                 ....*...
gi 15599169  627 HESRPGQG 634
Cdd:PRK10337 435 FGNAPEGG 442
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
606-641 1.91e-04

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 42.95  E-value: 1.91e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15599169 606 GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16916 142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
502-643 2.25e-04

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 41.82  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 502 RAQYAPRVEEKGLRFALQLDdsLPDTlegDAGKLAQALGYLVDNAIK----FTARGSVTLRVAAGRTHdgvaLRVEVIDT 577
Cdd:COG2172   7 DLEDLGLARRAVRALLRELG--LDED---DADDLVLAVSEAVTNAVRhaygGDPDGPVEVELELDPDG----LEIEVRDE 77
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599169 578 GIGFDMAagsdlyqRFVQADSSLTRGygglGIGLALCRKLVEllggELTHESRPGqGSRFLLRLQL 643
Cdd:COG2172  78 GPGFDPE-------DLPDPYSTLAEG----GRGLFLIRRLMD----EVEYESDPG-GTTVRLVKRL 127
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
375-626 2.81e-04

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 44.29  E-value: 2.81e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 375 EVGLLSLALADRINAMKEERARILQESSRKLEALNQELANSNRLKDEF--------LATVTHELRTP---MSGVIGSLEL 443
Cdd:COG4192 381 EIGRIARLLRVFRDQAIEKTQELETEIEERKRIEKNLRQTQDELIQAAkmavvgqtMTSLAHELNQPlnaMSMYLFSAKK 460
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 444 MQTVPMDVELAEYQRTAAGSARDMMRMVNDILALIELQAGKLyprrEPFSLRGLFDSLRAQYAPRveEKGLRFALQLDDS 523
Cdd:COG4192 461 ALEQENYAQLPTSLDKIEGLIERMDKIIKSLRQFSRKSDTPL----QPVDLRQVIEQAWELVESR--AKPQQITLHIPDD 534
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 524 LPdtLEGDAGKLAQALGYLVDN---AIKFTARGSVTLRVAAGRthdgvaLRVEVIDTGIGFDMAagSDLYQRFVqadssl 600
Cdd:COG4192 535 LM--VQGDQVLLEQVLVNLLVNaldAVATQPQISVDLLSNAEN------LRVAISDNGNGWPLV--DKLFTPFT------ 598
                       250       260
                ....*....|....*....|....*.
gi 15599169 601 TRGYGGLGIGLALCRKLVELLGGELT 626
Cdd:COG4192 599 TTKEVGLGLGLSICRSIMQQFGGDLY 624
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
530-643 3.48e-04

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 40.72  E-value: 3.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 530 GDAGKLAQALGYLVDNAIKFT--ARGSVTLRVAAGRTH--DGVA---LRVEVIDTGIGFDMAAGSDLYQRfvqadsslTR 602
Cdd:cd16932   2 GDQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTKKQigDGVHvihLEFRITHPGQGLPEELVQEMFEE--------NQ 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15599169 603 GYGGLGIGLALCRKLVELLGGELTHeSRPGQGSRFLLRLQL 643
Cdd:cd16932  74 WTTQEGLGLSISRKLVKLMNGDVRY-LREAGRSYFLITLEL 113
glnL PRK11073
nitrogen regulation protein NR(II);
428-632 9.30e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 42.38  E-value: 9.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  428 HELRTPMSGVIGSLELMQTVPMDVELAEYQRTAAGSArDMMRmvndilALIELQAGKLYP-RREPFSLRGLFDSLRAQYA 506
Cdd:PRK11073 139 HEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQA-DRLR------NLVDRLLGPQRPgTHVTESIHKVAERVVQLVS 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  507 PRVEEKgLRFALQLDDSLPDtLEGDAGKLAQALGYLVDNAIKFTAR--GSVTL--RVAAGRTHDGV----ALRVEVIDTG 578
Cdd:PRK11073 212 LELPDN-VRLIRDYDPSLPE-LAHDPDQIEQVLLNIVRNALQALGPegGTITLrtRTAFQLTLHGEryrlAARIDIEDNG 289
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15599169  579 IGFDMAAGSDLYQRFVQADSsltrgyGGLGIGLALCRKLVELLGGELTHESRPG 632
Cdd:PRK11073 290 PGIPPHLQDTLFYPMVSGRE------GGTGLGLSIARNLIDQHSGKIEFTSWPG 337
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
606-644 1.94e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 41.71  E-value: 1.94e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 15599169 606 GLGIGLALCRKLVELLGGELTHESRPGQGSRFLLRLQLT 644
Cdd:COG0643 381 GRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLT 419
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
531-628 1.98e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 38.60  E-value: 1.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 531 DAGKLAQALGYLVDNAIKFT-ARGSVTLRVAagrtHDGVALRVEVIDTGIGFDMAAGSDLYQRFVQADSSLTRGyGGLGI 609
Cdd:cd16975   1 DTLLLSRALINIISNACQYApEGGTVSISIY----DEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYGM 75
                        90
                ....*....|....*....
gi 15599169 610 GLALCRKLVELLGGELTHE 628
Cdd:cd16975  76 GLYIAKNLVEKHGGSLIIE 94
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
670-777 2.01e-03

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.83  E-value: 2.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAiNQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGFATCRAIRALPGCAELPVLALta 749
Cdd:cd17539   1 VLLVDDRP-SSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPILAV-- 77
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 750 hSHSGDRERCLAA---GMSDYMAKPVKFEEL 777
Cdd:cd17539  78 -ADPGDRGRLIRAleiGVNDYLVRPIDPNEL 107
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
535-641 2.11e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 38.21  E-value: 2.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 535 LAQALGYLVDNAikFTARGSVT---LRVAAGRTHDGVALRVEviDTGIGFDMAAGSDLYQRFVQadsslTRGYG-GLGIG 610
Cdd:cd16976   1 IQQVLMNLLQNA--LDAMGKVEnprIRIAARRLGGRLVLVVR--DNGPGIAEEHLSRVFDPFFT-----TKPVGkGTGLG 71
                        90       100       110
                ....*....|....*....|....*....|.
gi 15599169 611 LALCRKLVELLGGELTHESRPGQGSRFLLRL 641
Cdd:cd16976  72 LSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
529-640 3.77e-03

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 38.12  E-value: 3.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 529 EGDAGKLAQALGYLVDNAIKFTARGSVTLRVAAGRTHdgVALRVEVIDTGIGFdmaagSDLyqrfvqaDSSLTRGY---G 605
Cdd:cd16934  20 EVRQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGR--VALEILAVDQGPGI-----ADV-------DEALRDGFstgG 85
                        90       100       110
                ....*....|....*....|....*....|....*
gi 15599169 606 GLGIGLALCRKLVellgGELTHESRPGQGSRFLLR 640
Cdd:cd16934  86 GLGLGLGGVRRLA----DEFDLHSAPGRGTVVVAR 116
Trep_Strep TIGR02185
putative ECF transporter S component, Trep_Strep family; This family consists of strongly ...
281-381 4.03e-03

putative ECF transporter S component, Trep_Strep family; This family consists of strongly hydrophobic proteins about 190 amino acids in length with a strongly basic motif near the C-terminus. If is found in rather few species, but in paralogous families of 12 members in the oral pathogenic spirochaete Treponema denticola and 2 in Streptococcus pneumoniae R6. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 274019  Cd Length: 189  Bit Score: 39.19  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169   281 LLALMAVGALVMLMALTMSYAVALRLATYLALAFTGLIfaAGILAWLRGMRVARYfiiaWTAFLLGGIvntLMVLGYLPN 360
Cdd:TIGR02185   8 FIGLLTAIYFAIQFIVGMLTMTTGFFAHLFSPGITAFL--VGIIFFLMVAKVPKR----GVIFIFGIL---LGLLFFLMG 78
                          90       100
                  ....*....|....*....|..
gi 15599169   361 MFLTM-YASQIGSALEVGLLSL 381
Cdd:TIGR02185  79 MYWPMiISSIIGGLLADIIAST 100
HATPase_RsbW-like cd16936
Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...
538-622 4.12e-03

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.


Pssm-ID: 340413 [Multi-domain]  Cd Length: 91  Bit Score: 37.25  E-value: 4.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 538 ALGYLVDNAIKFTARGSVTLRVAAGRTHDGVALRVEVIDTGIGFDMAAGsdlyqrfvqADSSLTRGYGGLgiGLALCRKL 617
Cdd:cd16936   4 AVSEAVTNAVRHAYRHDGPGPVRLELDLDPDRLRVEVTDSGPGFDPLRP---------ADPDAGLREGGR--GLALIRAL 72

                ....*
gi 15599169 618 VELLG 622
Cdd:cd16936  73 MDEVG 77
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
670-771 5.18e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 37.10  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169 670 VLVVEDNAINQLVTRGMLLKLGYRVRTADNGSEALELLARERPDGVLLDCQMPVMDGF-ATCRAIRALPGcaeLPVLALT 748
Cdd:cd19928   1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLdLIPRIKKARPD---LPIIVMS 77
                        90       100
                ....*....|....*....|...
gi 15599169 749 AHSHSGDRERCLAAGMSDYMAKP 771
Cdd:cd19928  78 AQNTLMTAVKAAERGAFEYLPKP 100
PRK09191 PRK09191
two-component response regulator; Provisional
670-749 6.45e-03

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 39.06  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599169  670 VLVVEDNAI-----NQLVTRgmllkLGYRV----RTADngsEALELLARERPDGVLLDCQMPvmDGFATCRAIRALPGCA 740
Cdd:PRK09191 140 VLIIEDEPIiamdlEQLVES-----LGHRVtgiaRTRA---EAVALAKKTRPGLILADIQLA--DGSSGIDAVNDILKTF 209

                 ....*....
gi 15599169  741 ELPVLALTA 749
Cdd:PRK09191 210 DVPVIFITA 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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